1P9K

THE SOLUTION STRUCTURE OF YBCJ FROM E. COLI REVEALS A RECENTLY DISCOVERED ALFAL MOTIF INVOLVED IN RNA-BINDING


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 60 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations,structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

The solution structure of YbcJ from Escherichia coli reveals a recently discovered alphaL motif involved in RNA binding.

Volpon, L.Lievre, C.Osborne, M.J.Gandhi, S.Iannuzzi, P.Larocque, R.Cygler, M.Gehring, K.Ekiel, I.

(2003) J Bacteriol 185: 4204-4210

  • DOI: https://doi.org/10.1128/JB.185.14.4204-4210.2003
  • Primary Citation of Related Structures:  
    1P9K

  • PubMed Abstract: 

    The structure of the recombinant Escherichia coli protein YbcJ, a representative of a conserved family of bacterial proteins (COG2501), was determined by nuclear magnetic resonance. The fold of YbcJ identified it as a member of the larger family of S4-like RNA binding domains. These domains bind to structured RNA, such as that found in tRNA, rRNA, and a pseudoknot of mRNA. The structure of YbcJ revealed a highly conserved patch of basic residues, comprising amino acids K26, K38, R55, K56, and K59, which likely participate in RNA binding.


  • Organizational Affiliation

    Department of Biochemistry, McGill University, Montreal, Quebec, H3G 1Y6, Canada.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
orf, hypothetical protein79Escherichia coli K-12Mutation(s): 0 
Gene Names: ybcJ
UniProt
Find proteins for P0AAS7 (Escherichia coli (strain K12))
Explore P0AAS7 
Go to UniProtKB:  P0AAS7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0AAS7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 60 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations,structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2003-11-25
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Source and taxonomy, Version format compliance