4UZM

Shotgun proteolysis: A practical application


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 20 
  • Selection Criteria: NO VIOLATIONS 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Solution Structure of a Soluble Fragment Derived from a Membrane Protein by Shotgun Proteolysis.

Allen, M.D.Christie, M.Jones, P.Porebski, B.T.Roome, B.Freund, S.M.Buckle, A.M.Bycroft, M.Christ, D.

(2015) Protein Eng Des Sel 28: 445

  • DOI: https://doi.org/10.1093/protein/gzv021
  • Primary Citation of Related Structures:  
    4UZM

  • PubMed Abstract: 

    We have previously reported a phage display method for the identification of protein domains on a genome-wide scale (shotgun proteolysis). Here we present the solution structure of a fragment of the Escherichia coli membrane protein yrfF, as identified by shotgun proteolysis, and determined by NMR spectroscopy. Despite the absence of computational predictions, the fragment formed a well-defined beta-barrel structure, distantly falling within the OB-fold classification. Our results highlight the potential of high-throughput experimental approaches for the identification of protein domains for structural studies.


  • Organizational Affiliation

    MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PUTATIVE MEMBRANE PROTEIN IGAA HOMOLOG120Escherichia coliMutation(s): 0 
UniProt
Find proteins for P45800 (Escherichia coli (strain K12))
Explore P45800 
Go to UniProtKB:  P45800
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP45800
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 20 
  • Conformers Submitted: 20 
  • Selection Criteria: NO VIOLATIONS 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-09-17
    Type: Initial release
  • Version 1.1: 2014-09-24
    Changes: Atomic model
  • Version 1.2: 2015-04-29
    Changes: Database references, Other
  • Version 1.3: 2015-10-21
    Changes: Database references
  • Version 1.4: 2016-04-27
    Changes: Atomic model, Other
  • Version 1.5: 2024-05-15
    Changes: Data collection, Database references, Other