5ERI

MarR Protein from Peptoclostridium difficile DA00132


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.250 
  • R-Value Work: 0.212 
  • R-Value Observed: 0.213 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of the multiple antibiotic resistance regulator MarR from Clostridium difficile.

Peng, J.W.Yuan, H.Tan, X.S.

(2017) Acta Crystallogr F Struct Biol Commun 73: 363-368

  • DOI: https://doi.org/10.1107/S2053230X1700766X
  • Primary Citation of Related Structures:  
    5ERI

  • PubMed Abstract: 

    Regulators of multiple antibiotic resistance (MarRs) are key players against toxins in prokaryotes. MarR homologues have been identified in many bacterial and archaeal species which pose daunting antibiotic resistance issues that threaten public health. The continuous prevalence of Clostridium difficile infection (CDI) throughout the world is associated with the abuse of antibiotics, and antibiotic treatments of CDI have limited effect. In the genome of C. difficile strain 630, the marR gene (ID 4913953) encodes a MarR protein. Here, MarR from C. difficile (MarR C.difficile ) was subcloned and crystallized for the first time. MarR C.difficile was successfully expressed in Escherichia coli in a soluble form and was purified to near-homogeneity (>95%) by a two-step purification protocol. The structure of MarR C.difficile has been solved at 2.3 Å resolution. The crystal belonged to the monoclinic space group P4 3 2 1 2, with unit-cell parameters a = b = 66.569, c = 83.654 Å. The structure reported reveals MarR C.difficile to be a dimer, with each subunit consisting of six α-helices and three antiparallel β-hairpins. MarR C.difficile shows high structural similarity to the MarR proteins from E. coli and Staphylococcus aureus, indicating that MarR C.difficile might be a DNA-binding protein.


  • Organizational Affiliation

    Department of Chemistry, Fudan University, 220 Handan Road, Shanghai 200433, People's Republic of China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MarR family transcriptional regulator169Clostridioides difficileMutation(s): 0 
Gene Names: yybA
UniProt
Find proteins for A0A031WDA8 (Clostridioides difficile)
Explore A0A031WDA8 
Go to UniProtKB:  A0A031WDA8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A031WDA8
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.250 
  • R-Value Work: 0.212 
  • R-Value Observed: 0.213 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 66.569α = 90
b = 66.569β = 90
c = 83.654γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data processing
MOLREPphasing
Cootmodel building

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Natural Science Fundation of ChinaChina21472027
National Natural Science Fundation of ChinaChina31270869

Revision History  (Full details and data files)

  • Version 1.0: 2016-11-16
    Type: Initial release
  • Version 1.1: 2017-06-14
    Changes: Database references
  • Version 1.2: 2020-01-01
    Changes: Database references
  • Version 1.3: 2023-11-08
    Changes: Data collection, Database references, Refinement description