1PA4

Solution structure of a putative ribosome-binding factor from Mycoplasma pneumoniae (MPN156)


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 16 
  • Selection Criteria: Submitted conformers are those with lowest DYANA target functions. 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Solution structure of a putative ribosome binding protein from Mycoplasma pneumoniae and comparison to a distant homolog.

Rubin, S.M.Pelton, J.G.Yokota, H.Kim, R.Wemmer, D.E.

(2003) J Struct Funct Genomics 4: 235-243

  • DOI: https://doi.org/10.1023/b:jsfg.0000016127.57320.82
  • Primary Citation of Related Structures:  
    1PA4

  • PubMed Abstract: 

    The solution structure of MPN156, a ribosome-binding factor A (RBFA) protein family member from Mycoplasma pneumoniae, is presented. The structure, solved by nuclear magnetic resonance, has a type II KH fold typical of RNA binding proteins. Despite only approximately 20% sequence identity between MPN156 and another family member from Escherichia coli, the two proteins have high structural similarity. The comparison demonstrates that many of the conserved residues correspond to conserved elements in the structures. Compared to a structure based alignment, standard alignment methods based on sequence alone mispair a majority of amino acids in the two proteins. Implications of these discrepancies for sequence based structural modeling are discussed.


  • Organizational Affiliation

    Department of Chemistry, University of California, Berkeley, CA 94720, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Probable ribosome-binding factor A116Mycoplasmoides pneumoniaeMutation(s): 0 
Gene Names: MPN156
UniProt
Find proteins for P75589 (Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1))
Explore P75589 
Go to UniProtKB:  P75589
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP75589
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 16 
  • Selection Criteria: Submitted conformers are those with lowest DYANA target functions. 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-03-02
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-23
    Changes: Database references, Derived calculations