2RV8

Solution Structure of the PhoP DNA-Binding Domain from Mycobacterium tuberculosis


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

Solution structure of the PhoP DNA-binding domain from Mycobacterium tuberculosis.

Macdonald, R.Sarkar, D.Amer, B.R.Clubb, R.T.

(2015) J Biomol NMR 63: 111-117

  • DOI: https://doi.org/10.1007/s10858-015-9965-0
  • Primary Citation of Related Structures:  
    2RV8

  • PubMed Abstract: 

    Tuberculosis caused by Mycobacterium tuberculosis is a leading cause of death world-wide. The PhoP protein is required for virulence and is part of the PhoPR two-component system that regulates gene expression. The NMR-derived solution structure of the PhoP C-terminal DNA-binding domain is reported. Residues 150 to 246 form a structured domain that contains a winged helix-turn-helix motif. We provide evidence that the transactivation loop postulated to contact RNA polymerase is partially disordered in solution, and that the polypeptide that connects the DNA-binding domain to the regulatory domain is unstructured.


  • Organizational Affiliation

    Department of Chemistry and Biochemistry, University of California, Los Angeles, 602 Boyer Hall, Los Angeles, CA, 90095, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DNA-binding response regulator128Mycobacterium tuberculosis CAS/NITR204Mutation(s): 0 
Gene Names: J113_05350
UniProt
Find proteins for P71814 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore P71814 
Go to UniProtKB:  P71814
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP71814
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: 2015-08-12
    Type: Initial release
  • Version 1.1: 2022-08-24
    Changes: Data collection, Database references
  • Version 1.2: 2023-06-14
    Changes: Other