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Q9LJL3

- PREP1_ARATH

UniProt

Q9LJL3 - PREP1_ARATH

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Protein

Presequence protease 1, chloroplastic/mitochondrial

Gene

PREP1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

ATP-independent protease that degrades both mitochondrial and chloroplastic transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, with a bias for positively charged amino acid residues.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Zn2+Note: Binds 1 zinc ion per subunit.
  • Mg2+Note: Binds 2 Magnesium ions per subunit.

Enzyme regulationi

Inactive in the absence of MgCl2 and CaCl2 and full activation at 10 mM concentrations of either ion. Completely inhibited by the metal chelator orthophenanthroline, but not affected by phenylmethylsulfonyl fluoride (PMSF) or N-ethylmaleimide (NEM).

pH dependencei

Active from pH 4 to 10.

Temperature dependencei

Optimum temperature is 28 degrees Celsius. Active from 4 to 40 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi162 – 1621Zinc; catalytic
Active sitei165 – 1651Proton acceptor
Metal bindingi166 – 1661Zinc; catalytic
Metal bindingi262 – 2621Zinc; catalytic

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: TAIR

GO - Biological processi

  1. protein processing Source: TAIR
  2. response to cadmium ion Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:GQT-1641-MONOMER.
ARA:GQT-1642-MONOMER.

Protein family/group databases

MEROPSiM16.012.

Names & Taxonomyi

Protein namesi
Recommended name:
Presequence protease 1, chloroplastic/mitochondrial (EC:3.4.24.-)
Short name:
AtPreP1
Short name:
PreP 1
Alternative name(s):
Zinc metalloprotease 1
Short name:
AtZnMP1
Gene namesi
Name:PREP1
Synonyms:ZNMP1
Ordered Locus Names:At3g19170
ORF Names:MVI11.6, MVI11.7, MVI11_8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G19170.

Subcellular locationi

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. chloroplast Source: TAIR
  3. chloroplast envelope Source: TAIR
  4. chloroplast stroma Source: TAIR
  5. mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Mitochondrion, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi162 – 1621H → L: Loss of activity. 1 Publication
Mutagenesisi165 – 1651E → Q: Loss of activity. 1 Publication
Mutagenesisi166 – 1661H → L: Loss of activity. 1 Publication
Mutagenesisi179 – 1791E → Q: Decreased activity toward some substrates. 1 Publication
Mutagenesisi194 – 1941N → A: Reduced activity. 1 Publication
Mutagenesisi240 – 2401E → Q: Decreased activity toward some substrates. 1 Publication
Mutagenesisi245 – 2451E → Q: No loss of activity. 1 Publication
Mutagenesisi256 – 2561K → C: Inactive under oxidizing conditions and fully active under reducing conditions; when associated with C-937. 1 Publication
Mutagenesisi262 – 2621E → Q: Loss of activity. 1 Publication
Mutagenesisi264 – 2641K → C: Inactive under oxidizing conditions and fully active under reducing conditions; when associated with C-895. 1 Publication
Mutagenesisi416 – 4161A → C: Little or no effect; when associated with C-700. 1 Publication
Mutagenesisi430 – 4301E → C: Inactive under oxidizing conditions and fully active under reducing conditions; when associated with C-767. 1 Publication
Mutagenesisi700 – 7001N → C: Little or no effect; when associated with C-416. 1 Publication
Mutagenesisi767 – 7671S → C: Inactive under oxidizing conditions and fully active under reducing conditions; when associated with C-430. 1 Publication
Mutagenesisi895 – 8951Q → C: Inactive under oxidizing conditions and fully active under reducing conditions; when associated with C-264. 1 Publication
Mutagenesisi933 – 9331R → A or K: Loss of activity. 1 Publication
Mutagenesisi937 – 9371G → C: Inactive under oxidizing conditions and fully active under reducing conditions; when associated with C-256. 1 Publication
Mutagenesisi939 – 9391Y → F: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8484Chloroplast and mitochondrionSequence AnalysisAdd
BLAST
Chaini85 – 1080996Presequence protease 1, chloroplastic/mitochondrialPRO_0000249938Add
BLAST

Proteomic databases

PaxDbiQ9LJL3.
PRIDEiQ9LJL3.

Expressioni

Tissue specificityi

Expressed only in siliques and flowers.1 Publication

Gene expression databases

ExpressionAtlasiQ9LJL3. baseline and differential.
GenevestigatoriQ9LJL3.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
ATPBP176146EBI-7143359,EBI-7143406From a different organism.

Protein-protein interaction databases

IntActiQ9LJL3. 4 interactions.
MINTiMINT-7231907.

Structurei

Secondary structure

1
1080
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi101 – 1044Combined sources
Beta strandi107 – 1159Combined sources
Turni116 – 1194Combined sources
Beta strandi120 – 1278Combined sources
Turni128 – 1303Combined sources
Beta strandi133 – 1386Combined sources
Beta strandi142 – 15110Combined sources
Beta strandi155 – 1584Combined sources
Helixi160 – 1678Combined sources
Helixi180 – 1878Combined sources
Beta strandi190 – 1934Combined sources
Beta strandi199 – 21012Combined sources
Helixi211 – 22616Combined sources
Helixi229 – 2313Combined sources
Helixi235 – 2406Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi254 – 2563Combined sources
Helixi258 – 2669Combined sources
Helixi270 – 28213Combined sources
Helixi287 – 2893Combined sources
Turni296 – 2983Combined sources
Helixi299 – 3013Combined sources
Helixi304 – 31411Combined sources
Helixi317 – 3193Combined sources
Beta strandi320 – 3289Combined sources
Helixi330 – 34112Combined sources
Helixi349 – 3524Combined sources
Beta strandi365 – 3728Combined sources
Beta strandi375 – 3773Combined sources
Helixi379 – 3813Combined sources
Beta strandi383 – 3908Combined sources
Helixi398 – 41215Combined sources
Helixi418 – 4258Combined sources
Beta strandi430 – 4323Combined sources
Beta strandi436 – 4383Combined sources
Beta strandi440 – 4434Combined sources
Beta strandi445 – 4539Combined sources
Helixi455 – 4573Combined sources
Helixi458 – 47518Combined sources
Helixi479 – 49517Combined sources
Helixi503 – 51513Combined sources
Turni516 – 5183Combined sources
Helixi523 – 5253Combined sources
Helixi528 – 54114Combined sources
Helixi543 – 55412Combined sources
Turni555 – 5573Combined sources
Beta strandi561 – 5699Combined sources
Helixi572 – 58918Combined sources
Helixi593 – 61018Combined sources
Helixi616 – 6194Combined sources
Helixi627 – 6293Combined sources
Beta strandi640 – 65314Combined sources
Beta strandi657 – 66711Combined sources
Turni673 – 6753Combined sources
Helixi676 – 6783Combined sources
Helixi679 – 68810Combined sources
Beta strandi692 – 6943Combined sources
Helixi696 – 70611Combined sources
Beta strandi707 – 71913Combined sources
Beta strandi722 – 73615Combined sources
Helixi737 – 7393Combined sources
Helixi740 – 75314Combined sources
Helixi759 – 77921Combined sources
Helixi781 – 79111Combined sources
Helixi795 – 80410Combined sources
Helixi806 – 82116Combined sources
Helixi823 – 83715Combined sources
Beta strandi844 – 8496Combined sources
Helixi851 – 86616Combined sources
Beta strandi888 – 8914Combined sources
Beta strandi895 – 90410Combined sources
Helixi905 – 9084Combined sources
Helixi915 – 92511Combined sources
Helixi927 – 9315Combined sources
Turni932 – 9365Combined sources
Beta strandi939 – 9468Combined sources
Turni947 – 9504Combined sources
Beta strandi951 – 96010Combined sources
Helixi963 – 9708Combined sources
Helixi972 – 9776Combined sources
Helixi983 – 99715Combined sources
Helixi1003 – 101513Combined sources
Helixi1020 – 103112Combined sources
Helixi1035 – 105117Combined sources
Beta strandi1053 – 10586Combined sources
Helixi1060 – 106910Combined sources
Turni1070 – 10723Combined sources
Beta strandi1074 – 10774Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FGEX-ray2.10A/B86-1080[»]
ProteinModelPortaliQ9LJL3.
SMRiQ9LJL3. Positions 100-1078.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9LJL3.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili571 – 61242Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M16 family. PreP subfamily.Curated

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

eggNOGiCOG1026.
HOGENOMiHOG000008829.
InParanoidiQ9LJL3.
KOiK06972.
OMAiANNERSN.
PhylomeDBiQ9LJL3.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
IPR013578. Peptidase_M16C_assoc.
[Graphical view]
PfamiPF08367. M16C_assoc. 1 hit.
PF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 4 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9LJL3-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLRTVSCLAS RSSSSLFFRF FRQFPRSYMS LTSSTAALRV PSRNLRRISS
60 70 80 90 100
PSVAGRRLLL RRGLRIPSAA VRSVNGQFSR LSVRAVATQP APLYPDVGQD
110 120 130 140 150
EAEKLGFEKV SEEFISECKS KAILFKHKKT GCEVMSVSNE DENKVFGVVF
160 170 180 190 200
RTPPKDSTGI PHILEHSVLC GSRKYPVKEP FVELLKGSLH TFLNAFTYPD
210 220 230 240 250
RTCYPVASTN TKDFYNLVDV YLDAVFFPKC VDDAHTFQQE GWHYELNDPS
260 270 280 290 300
EDISYKGVVF NEMKGVYSQP DNILGRIAQQ ALSPENTYGV DSGGDPKDIP
310 320 330 340 350
NLTFEEFKEF HRQYYHPSNA RIWFYGDDDP VHRLRVLSEY LDMFEASPSP
360 370 380 390 400
NSSKIKFQKL FSEPVRLVEK YPAGRDGDLK KKHMLCVNWL LSEKPLDLQT
410 420 430 440 450
QLALGFLDHL MLGTPASPLR KILLESGLGE ALVSSGLSDE LLQPQFGIGL
460 470 480 490 500
KGVSEENVQK VEELIMDTLK KLAEEGFDND AVEASMNTIE FSLRENNTGS
510 520 530 540 550
FPRGLSLMLQ SISKWIYDMD PFEPLKYTEP LKALKTRIAE EGSKAVFSPL
560 570 580 590 600
IEKLILNNSH RVTIEMQPDP EKATQEEVEE KNILEKVKAA MTEEDLAELA
610 620 630 640 650
RATEELKLKQ ETPDPPEALR CVPSLNLGDI PKEPTYVPTE VGDINGVKVL
660 670 680 690 700
RHDLFTNDII YTEVVFDIGS LKHELLPLVP LFCQSLLEMG TKDLTFVQLN
710 720 730 740 750
QLIGRKTGGI SVYPLTSSVR GKDEPCSKII VRGKSMAGRA DDLFNLMNCL
760 770 780 790 800
LQEVQFTDQQ RFKQFVSQSR ARMENRLRGS GHGIAAARMD AMLNIAGWMS
810 820 830 840 850
EQMGGLSYLE FLHTLEKKVD EDWEGISSSL EEIRRSLLAR NGCIVNMTAD
860 870 880 890 900
GKSLTNVEKS VAKFLDLLPE NPSGGLVTWD GRLPLRNEAI VIPTQVNYVG
910 920 930 940 950
KAGNIYSTGY ELDGSAYVIS KHISNTWLWD RVRVSGGAYG GFCDFDSHSG
960 970 980 990 1000
VFSYLSYRDP NLLKTLDIYD GTGDFLRGLD VDQETLTKAI IGTIGDVDSY
1010 1020 1030 1040 1050
QLPDAKGYSS LLRHLLGVTD EERQRKREEI LTTSLKDFKD FAQAIDVVRD
1060 1070 1080
KGVAVAVASA EDIDAANNER SNFFEVKKAL
Length:1,080
Mass (Da):121,015
Last modified:September 19, 2006 - v2
Checksum:i9FD259970195B9FC
GO

Sequence cautioni

The sequence BAB02957.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP000419 Genomic DNA. Translation: BAB02957.1. Different initiation.
CP002686 Genomic DNA. Translation: AEE76201.1.
AY090240 mRNA. Translation: AAL90904.1.
AY091051 mRNA. Translation: AAM13872.1.
BT006362 mRNA. Translation: AAP21170.1.
BT002372 mRNA. Translation: AAN86205.1.
RefSeqiNP_188548.2. NM_112804.4. [Q9LJL3-1]
UniGeneiAt.27915.

Genome annotation databases

EnsemblPlantsiAT3G19170.1; AT3G19170.1; AT3G19170. [Q9LJL3-1]
GeneIDi821451.
KEGGiath:AT3G19170.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP000419 Genomic DNA. Translation: BAB02957.1 . Different initiation.
CP002686 Genomic DNA. Translation: AEE76201.1 .
AY090240 mRNA. Translation: AAL90904.1 .
AY091051 mRNA. Translation: AAM13872.1 .
BT006362 mRNA. Translation: AAP21170.1 .
BT002372 mRNA. Translation: AAN86205.1 .
RefSeqi NP_188548.2. NM_112804.4. [Q9LJL3-1 ]
UniGenei At.27915.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FGE X-ray 2.10 A/B 86-1080 [» ]
ProteinModelPortali Q9LJL3.
SMRi Q9LJL3. Positions 100-1078.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9LJL3. 4 interactions.
MINTi MINT-7231907.

Protein family/group databases

MEROPSi M16.012.

Proteomic databases

PaxDbi Q9LJL3.
PRIDEi Q9LJL3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G19170.1 ; AT3G19170.1 ; AT3G19170 . [Q9LJL3-1 ]
GeneIDi 821451.
KEGGi ath:AT3G19170.

Organism-specific databases

GeneFarmi 2137. 225.
TAIRi AT3G19170.

Phylogenomic databases

eggNOGi COG1026.
HOGENOMi HOG000008829.
InParanoidi Q9LJL3.
KOi K06972.
OMAi ANNERSN.
PhylomeDBi Q9LJL3.

Enzyme and pathway databases

BioCyci ARA:GQT-1641-MONOMER.
ARA:GQT-1642-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q9LJL3.
PROi Q9LJL3.

Gene expression databases

ExpressionAtlasi Q9LJL3. baseline and differential.
Genevestigatori Q9LJL3.

Family and domain databases

Gene3Di 3.30.830.10. 2 hits.
InterProi IPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
IPR013578. Peptidase_M16C_assoc.
[Graphical view ]
Pfami PF08367. M16C_assoc. 1 hit.
PF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view ]
SUPFAMi SSF63411. SSF63411. 4 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
    Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
    DNA Res. 7:217-221(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants."
    Staahl A., Moberg P., Ytterberg J., Panfilov O., Brockenhuus Von Lowenhielm H., Nilsson F., Glaser E.
    J. Biol. Chem. 277:41931-41939(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  5. "Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts."
    Moberg P., Staahl A., Bhushan S., Wright S.J., Eriksson A., Bruce B.D., Glaser E.
    Plant J. 36:616-628(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF HIS-162; GLU-165; HIS-166; GLU-240 AND GLU-245, SUBCELLULAR LOCATION.
  6. "Catalysis, subcellular localization, expression and evolution of the targeting peptides degrading protease, AtPreP2."
    Bhushan S., Staahl A., Nilsson S., Lefebvre B., Seki M., Roth C., McWilliam D., Wright S.J., Liberles D.A., Shinozaki K., Bruce B.D., Boutry M., Glaser E.
    Plant Cell Physiol. 46:985-996(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  7. "Two novel targeting peptide degrading proteases, PrePs, in mitochondria and chloroplasts, so similar and still different."
    Staahl A., Nilsson S., Lundberg P., Bhushan S., Biverstaahl H., Moberg P., Morisset M., Vener A., Maeler L., Langel U., Glaser E.
    J. Mol. Biol. 349:847-860(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE SPECIFICITY.
  8. "The closed structure of presequence protease PreP forms a unique 10,000 Angstroms3 chamber for proteolysis."
    Johnson K.A., Bhushan S., Staahl A., Hallberg B.M., Frohn A., Glaser E., Eneqvist T.
    EMBO J. 25:1977-1986(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 86-1080, MUTAGENESIS OF GLU-179; ASN-194; LYS-256; GLU-262; LYS-264; ALA-416; GLU-430; ASN-700; SER-767; GLN-895; ARG-933; GLY-937 AND TYR-939.

Entry informationi

Entry nameiPREP1_ARATH
AccessioniPrimary (citable) accession number: Q9LJL3
Secondary accession number(s): Q8RUN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: September 19, 2006
Last modified: November 26, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The 2 enzymes halves enclose a large proteolytic chamber spacious enough to hold peptide substrates, but sufficiently small to exclude larger, folded proteins. Since the active site includes residues from both the N- and C-terminal part of the protein, proteolysis can occur only when the chamber is closed. Covalently locking the 2 halves of the protease with disulfide bonds induces a loss of activity.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3