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Protein

Coat protein

Gene
N/A
Organism
Enterobacteria phage MS2 (Bacteriophage MS2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Forms the phage shell; binds to the phage RNA.

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Coat protein
OrganismiEnterobacteria phage MS2 (Bacteriophage MS2)
Taxonomic identifieri329852 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageLeviviridaeLevivirus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000002127 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, T=3 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved; by host
Chaini2 – 130129Coat proteinPRO_0000164843Add
BLAST

Interactioni

Subunit structurei

The shell is composed of 180 copies of the coat protein. The coat protein form dimers that assemble by group of 5. Twelve such pentamers are linked together with free dimers.

Protein-protein interaction databases

DIPiDIP-37669N.

Structurei

Secondary structure

1
130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114Combined sources
Beta strandi13 – 175Combined sources
Beta strandi19 – 279Combined sources
Beta strandi30 – 345Combined sources
Beta strandi38 – 403Combined sources
Beta strandi44 – 5310Combined sources
Beta strandi56 – 6510Combined sources
Beta strandi70 – 756Combined sources
Beta strandi79 – 835Combined sources
Beta strandi85 – 9410Combined sources
Beta strandi95 – 973Combined sources
Helixi99 – 11214Combined sources
Helixi118 – 1258Combined sources
Beta strandi126 – 1294Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQ3X-ray2.80A/B/C2-130[»]
1AQ4X-ray3.00A/B/C2-130[»]
1BMSX-ray2.70A/B/C2-130[»]
1MSCX-ray2.00A2-130[»]
1MSTX-ray2.60A/B/C2-130[»]
1MVAX-ray3.00A/B/C2-130[»]
1MVBX-ray3.00A/B/C2-130[»]
1U1YX-ray2.85A/B/C2-130[»]
1ZDHX-ray2.70A/B/C2-130[»]
1ZDIX-ray2.70A/B/C2-130[»]
1ZDJX-ray2.90A/B/C2-130[»]
1ZDKX-ray2.86A/B/C2-130[»]
1ZSEX-ray3.00A/B/C2-130[»]
2B2DX-ray2.90A/B/C2-130[»]
2B2EX-ray3.15A/B/C2-130[»]
2B2GX-ray3.02A/B/C2-130[»]
2BNYX-ray3.00A/B/C2-130[»]
2BQ5X-ray2.91A/B/C2-130[»]
2BS0X-ray2.45A/B/C2-130[»]
2BS1X-ray2.80A/B/C2-130[»]
2BU1X-ray2.20A/B/C2-130[»]
2C4QX-ray2.38A/B/C2-130[»]
2C4YX-ray2.68A/B/C2-130[»]
2C4ZX-ray2.60A/B/C2-130[»]
2C50X-ray2.65A/B/C2-130[»]
2C51X-ray2.80A/B/C2-130[»]
2IZ8X-ray3.30A/B/C2-130[»]
2IZ9X-ray2.85A/B/C2-130[»]
2IZMX-ray2.70A/B/C2-130[»]
2IZNX-ray2.56A/B/C2-130[»]
2MS2X-ray2.80A/B/C2-130[»]
2VTUX-ray3.50J/L2-130[»]
2WBHX-ray4.70A/B/C2-130[»]
4BP7electron microscopy39.00A0/A1/A2/A3/A4/A5/A6/A7/A8/A9/AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/AP/AQ/AR/AS/AT/AU/AV/AW/AX/AY/AZ/Aa/Ab/Ac/Ad/Ae/Af/Ag/Ah/Ai/Aj/Ak/Al/Am/An/Ao/Ap/Aq/Ar/As/At/Au/Av/Aw/Ax/B0/B1/B2/B3/B4/B5/B6/B7/B8/B9/BA2-130[»]
5MSFX-ray2.80A/B/C2-130[»]
6MSFX-ray2.80A/B/C2-130[»]
7MSFX-ray2.80A/B/C2-130[»]
ProteinModelPortaliP03612.
SMRiP03612. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03612.

Family & Domainsi

Family and domain databases

Gene3Di3.30.380.10. 1 hit.
InterProiIPR002703. Levivir_coat.
IPR015954. Phage_RNA-type_capsid.
[Graphical view]
PfamiPF01819. Levi_coat. 1 hit.
[Graphical view]
SUPFAMiSSF55405. SSF55405. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P03612-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASNFTQFVL VDNGGTGDVT VAPSNFANGV AEWISSNSRS QAYKVTCSVR
60 70 80 90 100
QSSAQNRKYT IKVEVPKVAT QTVGGVELPV AAWRSYLNME LTIPIFATNS
110 120 130
DCELIVKAMQ GLLKDGNPIP SAIAANSGIY
Length:130
Mass (Da):13,860
Last modified:January 23, 2007 - v2
Checksum:iABCDD9FD8B188C6A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00642 mRNA. Translation: CAA23989.1.
PIRiB04222. VCBPM2.
RefSeqiNP_040648.1. NC_001417.2.

Genome annotation databases

GeneIDi1260899.
KEGGivg:1260899.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure assembled from a chemically modified RNA genome hairpin variant

Virus Particle ExploreR db

Icosahedral capsid structure assembled from a modified RNA genome hairpin variant G7

Virus Particle ExploreR db

Icosahedral capsid structure assembled from modified RNA genome hairpin variant G10

Virus Particle ExploreR db

Icosahedral capsid structure assembled from modified RNA genome hairpin variant C10

Virus Particle ExploreR db

Icosahedral capsid structure of mutant E77D

Virus Particle ExploreR db

Icosahedral capsid structure of mutant T60S

Virus Particle ExploreR db

Icosahedral capsid structure of mutant T46A

Virus Particle ExploreR db

Icosahedral capsid structure of mutant T46A

Virus Particle ExploreR db

Icosahedral capsid structure of mutant T60S

Virus Particle ExploreR db

Icosahedral capsid structure of mutant P79N

Virus Particle ExploreR db

Icosahedral capsid structure associated with 8 nt RNA

Virus Particle ExploreR db

Icosahedral capsid structure associated with 19 nt RNA

Virus Particle ExploreR db

Icosahedral capsid structure associated with 19 nt RNA

Virus Particle ExploreR db

Icosahedral capsid structure associated with 23 nt RNA

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure associated with a aptamer RNA

Virus Particle ExploreR db

Icosahedral capsid structure associated with a F5 aptamer RNA

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00642 mRNA. Translation: CAA23989.1.
PIRiB04222. VCBPM2.
RefSeqiNP_040648.1. NC_001417.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQ3X-ray2.80A/B/C2-130[»]
1AQ4X-ray3.00A/B/C2-130[»]
1BMSX-ray2.70A/B/C2-130[»]
1MSCX-ray2.00A2-130[»]
1MSTX-ray2.60A/B/C2-130[»]
1MVAX-ray3.00A/B/C2-130[»]
1MVBX-ray3.00A/B/C2-130[»]
1U1YX-ray2.85A/B/C2-130[»]
1ZDHX-ray2.70A/B/C2-130[»]
1ZDIX-ray2.70A/B/C2-130[»]
1ZDJX-ray2.90A/B/C2-130[»]
1ZDKX-ray2.86A/B/C2-130[»]
1ZSEX-ray3.00A/B/C2-130[»]
2B2DX-ray2.90A/B/C2-130[»]
2B2EX-ray3.15A/B/C2-130[»]
2B2GX-ray3.02A/B/C2-130[»]
2BNYX-ray3.00A/B/C2-130[»]
2BQ5X-ray2.91A/B/C2-130[»]
2BS0X-ray2.45A/B/C2-130[»]
2BS1X-ray2.80A/B/C2-130[»]
2BU1X-ray2.20A/B/C2-130[»]
2C4QX-ray2.38A/B/C2-130[»]
2C4YX-ray2.68A/B/C2-130[»]
2C4ZX-ray2.60A/B/C2-130[»]
2C50X-ray2.65A/B/C2-130[»]
2C51X-ray2.80A/B/C2-130[»]
2IZ8X-ray3.30A/B/C2-130[»]
2IZ9X-ray2.85A/B/C2-130[»]
2IZMX-ray2.70A/B/C2-130[»]
2IZNX-ray2.56A/B/C2-130[»]
2MS2X-ray2.80A/B/C2-130[»]
2VTUX-ray3.50J/L2-130[»]
2WBHX-ray4.70A/B/C2-130[»]
4BP7electron microscopy39.00A0/A1/A2/A3/A4/A5/A6/A7/A8/A9/AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/AP/AQ/AR/AS/AT/AU/AV/AW/AX/AY/AZ/Aa/Ab/Ac/Ad/Ae/Af/Ag/Ah/Ai/Aj/Ak/Al/Am/An/Ao/Ap/Aq/Ar/As/At/Au/Av/Aw/Ax/B0/B1/B2/B3/B4/B5/B6/B7/B8/B9/BA2-130[»]
5MSFX-ray2.80A/B/C2-130[»]
6MSFX-ray2.80A/B/C2-130[»]
7MSFX-ray2.80A/B/C2-130[»]
ProteinModelPortaliP03612.
SMRiP03612. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-37669N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1260899.
KEGGivg:1260899.

Miscellaneous databases

EvolutionaryTraceiP03612.

Family and domain databases

Gene3Di3.30.380.10. 1 hit.
InterProiIPR002703. Levivir_coat.
IPR015954. Phage_RNA-type_capsid.
[Graphical view]
PfamiPF01819. Levi_coat. 1 hit.
[Graphical view]
SUPFAMiSSF55405. SSF55405. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of the gene coding for the bacteriophage MS2 coat protein."
    Min Jou W., Haegeman G., Ysebaert M., Fiers W.
    Nature 237:82-88(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The three-dimensional structure of the bacterial virus MS2."
    Valegaard K., Liljas L., Fridborg K., Unge T.
    Nature 345:36-41(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
  3. "Structure determination of the bacteriophage MS2."
    Valegard K., Liljas L., Fridborg K., Unge T.
    Acta Crystallogr. B 47:949-960(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
  4. "The refined structure of bacteriophage MS2 at 2.8-A resolution."
    Golmohammadi R., Valegaard K., Fridborg K., Liljas L.
    J. Mol. Biol. 234:620-639(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  5. "Crystal structure of an RNA bacteriophage coat protein-operator complex."
    Valegaard K., Murray J.B., Sotckley P.G., Stonehouse N.J., Liljas L.
    Nature 371:623-626(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  7. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH RNA.
  8. "Crystal structures of a series of RNA aptamers complexed to the same protein target."
    Rowsell S., Stonehouse N.J., Convery M.A., Adams C.J., Ellington A.D., Hirao I., Peabody D.S., Stockley P.G., Phillips S.E.
    Nat. Struct. Biol. 5:970-975(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiCOAT_BPMS2
AccessioniPrimary (citable) accession number: P03612
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 14, 2015
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.