2K4B

CopR Repressor Structure


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 350 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The copper-responsive repressor CopR of Lactococcus lactis is a 'winged helix' protein.

Cantini, F.Banci, L.Solioz, M.

(2009) Biochem J 417: 493-499

  • DOI: https://doi.org/10.1042/BJ20081713
  • Primary Citation of Related Structures:  
    2K4B

  • PubMed Abstract: 

    CopR of Lactococcus lactis is a copper-responsive repressor involved in copper homoeostasis. It controls the expression of a total of 11 genes, the CopR regulon, in a copper-dependent manner. In the absence of copper, CopR binds to the promoters of the CopR regulon. Copper releases CopR from the promoters, allowing transcription of the downstream genes to proceed. CopR binds through its N-terminal domain to a 'cop box' of consensus TACANNTGTA, which is conserved in Firmicutes. We have solved the NMR solution structure of the N-terminal DNA-binding domain of CopR. The protein fold has a winged helix structure resembling that of the BlaI repressor which regulates antibiotic resistance in Bacillus licheniformis. CopR differs from other copper-responsive repressors, and the present structure represents a novel family of copper regulators, which we propose to call the CopY family.


  • Organizational Affiliation

    Department of Chemistry and Magnetic Resonance Center, University of Florence, Sesto Fiorentino, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Transcriptional regulator99Lactococcus lactis subsp. lactisMutation(s): 0 
Gene Names: copRLL0832L451L45109
UniProt
Find proteins for Q9CHA6 (Lactococcus lactis subsp. lactis (strain IL1403))
Explore Q9CHA6 
Go to UniProtKB:  Q9CHA6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9CHA6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 350 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-01-27
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2022-03-16
    Changes: Data collection, Database references, Derived calculations
  • Version 1.3: 2024-05-29
    Changes: Data collection