2L04

The Solution Structure of the C-terminal Ig-like Domain of the Bacteriophage Lambda Tail Tube Protein


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 1.3 of the entry. See complete history


Literature

The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage l Tail Tube Protein.

Pell, L.G.Gasmi-Seabrook, G.M.Morais, M.Neudecker, P.Kanelis, V.Bona, D.Donaldson, L.W.Edwards, A.M.Howell, P.L.Davidson, A.R.Maxwell, K.L.

(2010) J Mol Biol 403: 468-479

  • DOI: https://doi.org/10.1016/j.jmb.2010.08.044
  • Primary Citation of Related Structures:  
    2L04

  • PubMed Abstract: 

    Immunoglobulin (Ig)-like domains are found frequently on the surface of tailed double-stranded DNA bacteriophages, yet their functional role remains obscure. Here, we have investigated the structure and function of the C-terminal Ig-like domain of gpV (gpV(C)), the tail tube protein of phage λ. This domain has been predicted through sequence similarity to be a member of the bacterial Ig-like domain 2 (Big_2) family, which is composed of more than 1300 phage and bacterial sequences. Using trypsin proteolysis, we have delineated the boundaries of gpV(C) and have shown that its removal reduces the biological activity of gpV by 100-fold; thus providing a definitive demonstration of a functional role for this domain. Determination of the solution structure of gpV(C) by NMR spectroscopy showed that it adopts a canonical Ig-like fold of the I-set class. This represents the first structure of a phage-encoded Ig-like domain and only the second structure of a Big_2 domain. Structural and sequence comparisons indicate that the gpV(C) structure is more representative of both the phage-encoded Big_2 domains and Big_2 domains in general than the other available Big_2 structure. Bioinformatics analyses have identified two conserved clusters of residues on the surface of gpV(C) that may be important in mediating the function of this domain.


  • Organizational Affiliation

    Department of Biochemistry, Faculty of Medicine, University of Toronto, Medical Sciences Building, Toronto, ON, Canada.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Major tail protein V91Lambdavirus lambdaMutation(s): 0 
Gene Names: V
UniProt
Find proteins for P03733 (Escherichia phage lambda)
Explore P03733 
Go to UniProtKB:  P03733
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03733
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: 2010-09-22
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2013-06-19
    Changes: Database references
  • Version 1.3: 2020-02-05
    Changes: Database references, Other