2K4K

Solution structure of GSP13 from Bacillus subtilis


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • 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 GSP13 from Bacillus subtilis exhibits an S1 domain related to cold shock proteins.

Yu, W.Hu, J.Yu, B.Xia, W.Jin, C.Xia, B.

(2009) J Biomol NMR 43: 255-259

  • DOI: https://doi.org/10.1007/s10858-009-9298-y
  • Primary Citation of Related Structures:  
    2K4K

  • PubMed Abstract: 

    GSP13 encoded by gene yugI is a sigma(B)-dependent general stress protein in Bacillus subtilis, which can be induced by heat shock, salt stress, ethanol stress, glucose starvation, oxidative stress and cold shock. Here we report the solution structure of GSP13 and it is the first structure of S1 domain containing protein in Bacillus subtilis. The structure of GSP13 mainly consists of a typical S1 domain along with a C-terminal 50-residue flexible tail, different from the other known S1 domain containing proteins. Comparison with other S1 domain structures reveals that GSP13 has a conserved RNA binding surface, and it may function similarly to cold shock proteins in response to cold stress.


  • Organizational Affiliation

    Beijing Nuclear Magnetic Resonance Center, College of Life Sciences, Peking University, Beijing 100871, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
General stress protein 13130Bacillus subtilisMutation(s): 0 
Gene Names: yugIBSU31390
UniProt
Find proteins for P80870 (Bacillus subtilis (strain 168))
Explore P80870 
Go to UniProtKB:  P80870
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP80870
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • 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: 2009-05-12
    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