5N7Y

Solution structure of B. subtilis Sigma G inhibitor CsfB


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 2.3 of the entry. See complete history


Literature

Structural and Functional Insights into Bacillus subtilis Sigma Factor Inhibitor, CsfB.

Martinez-Lumbreras, S.Alfano, C.Evans, N.J.Collins, K.M.Flanagan, K.A.Atkinson, R.A.Krysztofinska, E.M.Vydyanath, A.Jackter, J.Fixon-Owoo, S.Camp, A.H.Isaacson, R.L.

(2018) Structure 26: 640-648.e5

  • DOI: https://doi.org/10.1016/j.str.2018.02.007
  • Primary Citation of Related Structures:  
    5N7Y

  • PubMed Abstract: 

    Global changes in bacterial gene expression can be orchestrated by the coordinated activation/deactivation of alternative sigma (σ) factor subunits of RNA polymerase. Sigma factors themselves are regulated in myriad ways, including via anti-sigma factors. Here, we have determined the solution structure of anti-sigma factor CsfB, responsible for inhibition of two alternative sigma factors, σ G and σ E , during spore formation by Bacillus subtilis. CsfB assembles into a symmetrical homodimer, with each monomer bound to a single Zn 2+ ion via a treble-clef zinc finger fold. Directed mutagenesis indicates that dimer formation is critical for CsfB-mediated inhibition of both σ G and σ E , and we have characterized these interactions in vitro. This work represents an advance in our understanding of how CsfB mediates inhibition of two alternative sigma factors to drive developmental gene expression in a bacterium.


  • Organizational Affiliation

    Department of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Anti-sigma-G factor GinA,
B [auth C]
49Bacillus subtilisMutation(s): 0 
Gene Names: csfBginyaaMBSU00240
UniProt
Find proteins for P37534 (Bacillus subtilis (strain 168))
Explore P37534 
Go to UniProtKB:  P37534
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP37534
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZN
Query on ZN

Download Ideal Coordinates CCD File 
C [auth A],
D [auth C]
ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
United Kingdom--

Revision History  (Full details and data files)

  • Version 1.0: 2018-02-28
    Type: Initial release
  • Version 2.0: 2018-03-21
    Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Experimental preparation
  • Version 2.1: 2018-04-11
    Changes: Data collection, Database references
  • Version 2.2: 2019-05-08
    Changes: Data collection
  • Version 2.3: 2023-06-14
    Changes: Data collection, Database references, Derived calculations, Other