2LC0

Rv0020c_Nter structure


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 30 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural Insight into the Mycobacterium tuberculosis Rv0020c Protein and Its Interaction with the PknB Kinase

Roumestand, C.Leiba, J.Galophe, N.Margeat, E.Padilla, A.Bessin, Y.Barthe, P.Molle, V.Cohen-Gonsaud, M.

(2011) Structure 19: 1525-1534

  • DOI: https://doi.org/10.1016/j.str.2011.07.011
  • Primary Citation of Related Structures:  
    2LC0, 2LC1

  • PubMed Abstract: 

    The protein Rv0020c from Mycobacterium tuberculosis, also called FhaA, is one of the major substrates of the essential Ser/Thr protein kinase (STPK) PknB. The protein is composed of three domains and is phosphorylated on a unique site in its N terminus. We solved the solution structure of both N- and C-terminal domains and demonstrated that the approximately 300 amino acids of the intermediate domain are not folded. We present evidence that the FHA, a phosphospecific binding domain, of Rv0020c does not interact with the phosphorylated catalytic domains of PknB, but with the phosphorylated juxtamembrane domain that links the catalytic domain to the mycobacterial membrane. We also demonstrated that the degree and the pattern of phosphorylation of this juxtamembrane domain modulates the affinity of the substrate (Rv0020c) toward its kinase (PknB).


  • Organizational Affiliation

    CNRS UMR 5048, Centre de Biochimie Structurale, 29, rue de Navacelles 34090 Montpellier, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Putative uncharacterized protein TB39.8132Mycobacterium tuberculosis H37RvMutation(s): 0 
Gene Names: Rv0020cTB39.8
UniProt
Find proteins for P71590 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore P71590 
Go to UniProtKB:  P71590
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP71590
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 30 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-11-02
    Type: Initial release
  • Version 1.1: 2023-06-14
    Changes: Data collection, Database references, Other
  • Version 1.2: 2024-05-29
    Changes: Data collection