Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
1 to 9 of 9  Show
  1. 1
    Smith D.R., Robison K.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  2. 2
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3992 other entries.

  3. 3
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2871 other entries.

  4. 4
    "Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase."
    Morris V.K., Izard T.
    Protein Sci. 13:2547-2552(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 1-157, SUBUNIT.
    Category: Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  5. 5
    "Preparation of the crystal complex of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis with Coenzyme A and investigation of its three-dimensional structure at 2.1-A frame resolution."
    Timofeev V.I., Smirnova E.A., Chupova L.A., Esipov R.S., Kuranova I.P.
    Crystallogr. Rep. 55:1050-1059(2010)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH THE NATURAL INHIBITOR COENZYME A, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT.
    Category: Function, Interaction, Structure.
    Strain: H37Rv.
    Source: UniProtKB/Swiss-Prot (reviewed).
  6. 6
    "Kinetic, thermodynamic, and structural insight into the mechanism of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis."
    Wubben T.J., Mesecar A.D.
    J. Mol. Biol. 404:202-219(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 1-157 IN COMPLEXES WITH PHOSPHOPANTETHEINE AND A NON-HYDROLYZABLE ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Category: Function, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  7. 7
    "Structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase in complex with the feedback inhibitor CoA reveals only one active-site conformation."
    Wubben T., Mesecar A.D.
    Acta Crystallogr. F 67:541-545(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 1-157 IN COMPLEX WITH THE NATURAL INHIBITOR COENZYME A, ACTIVITY REGULATION.
    Category: Function, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  8. 8
    "X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis during the catalyzed reaction."
    Timofeev V., Smirnova E., Chupova L., Esipov R., Kuranova I.
    Acta Crystallogr. D 68:1660-1670(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) IN THE APO FORM AND IN COMPLEX WITH ATP.
    Category: Interaction, Structure.
    Strain: H37Rv.
    Source: UniProtKB/Swiss-Prot (reviewed).
  9. 9
    "Three-dimensional structure of phosphopantetheine adenylyltransferase from Mycobacterium Tuberculosis in the apo form and in complexes with coenzyme A and dephosphocoenzyme A."
    Timofeev V.I., Smirnova E.A., Chupova L.A., Esipov R.S., Kuranova I.P.
    Crystallogr. Rep. 57:96-104(2012)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 1-157 IN THE APO FORM AND IN COMPLEXES WITH COA AND 3'-DEPHOSPHO-COA.
    Category: Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
1 to 9 of 9  Show
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again