2JVW

Solution NMR structure of uncharacterized protein Q5E7H1 from Vibrio fischeri. Northeast Structural Genomics target VfR117


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 1.5 of the entry. See complete history


Literature

Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.

Aramini, J.M.Rossi, P.Fischer, M.Xiao, R.Acton, T.B.Montelione, G.T.

(2011) Proteins 79: 2988-2991

  • DOI: https://doi.org/10.1002/prot.23121
  • Primary Citation of Related Structures:  
    2JVW

  • PubMed Abstract: 

    Protein domain family PF09905 (DUF2132) is a family of small domains of unknown function that are conserved in a wide range of bacteria. Here we describe the solution NMR structure of the 80-residue VF0530 protein from Vibrio fischeri, the first structural representative from this protein domain family. We demonstrate that the structure of VF0530 adopts a unique four-helix motif that shows some similarity to the C-terminal double-stranded DNA (dsDNA) binding domain of RecA, as well as other nucleic acid binding domains. Moreover, gel shift binding data indicate a potential dsDNA binding role for VF0530.


  • Organizational Affiliation

    Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, USA. jma@cabm.rutgers.edu


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Uncharacterized protein88Aliivibrio fischeri ES114Mutation(s): 0 
Gene Names: VF0530
UniProt
Find proteins for Q5E7H1 (Aliivibrio fischeri (strain ATCC 700601 / ES114))
Explore Q5E7H1 
Go to UniProtKB:  Q5E7H1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5E7H1
Sequence Annotations
Expand
  • 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 

Revision History  (Full details and data files)

  • Version 1.0: 2007-10-16
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.2: 2011-08-03
    Changes: Database references
  • Version 1.3: 2011-09-21
    Changes: Database references
  • Version 1.4: 2020-02-19
    Changes: Data collection, Database references, Other
  • Version 1.5: 2023-06-14
    Changes: Database references, Other