1ZCE

X-Ray Crystal Structure of Protein Atu2648 from Agrobacterium tumefaciens. Northeast Structural Genomics Consortium Target AtR33.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.30 Å
  • R-Value Free: 0.211 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.195 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural genomics reveals EVE as a new ASCH/PUA-related domain.

Bertonati, C.Punta, M.Fischer, M.Yachdav, G.Forouhar, F.Zhou, W.Kuzin, A.P.Seetharaman, J.Abashidze, M.Ramelot, T.A.Kennedy, M.A.Cort, J.R.Belachew, A.Hunt, J.F.Tong, L.Montelione, G.T.Rost, B.

(2009) Proteins 75: 760-773

  • DOI: https://doi.org/10.1002/prot.22287
  • Primary Citation of Related Structures:  
    1ZCE, 2EVE, 2G2X, 2GBS

  • PubMed Abstract: 

    We report on several proteins recently solved by structural genomics consortia, in particular by the Northeast Structural Genomics consortium (NESG). The proteins considered in this study differ substantially in their sequences but they share a similar structural core, characterized by a pseudobarrel five-stranded beta sheet. This core corresponds to the PUA domain-like architecture in the SCOP database. By connecting sequence information with structural knowledge, we characterize a new subgroup of these proteins that we propose to be distinctly different from previously described PUA domain-like domains such as PUA proper or ASCH. We refer to these newly defined domains as EVE. Although EVE may have retained the ability of PUA domains to bind RNA, the available experimental and computational data suggests that both the details of its molecular function and its cellular function differ from those of other PUA domain-like domains. This study of EVE and its relatives illustrates how the combination of structure and genomics creates new insights by connecting a cornucopia of structures that map to the same evolutionary potential. Primary sequence information alone would have not been sufficient to reveal these evolutionary links.


  • Organizational Affiliation

    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. claudia.bertonati@uniroma1.it


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
hypothetical protein Atu2648155Agrobacterium fabrum str. C58Mutation(s): 7 
Gene Names: locus_tag="Atu2648"
UniProt
Find proteins for A9CHJ4 (Agrobacterium fabrum (strain C58 / ATCC 33970))
Explore A9CHJ4 
Go to UniProtKB:  A9CHJ4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA9CHJ4
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.30 Å
  • R-Value Free: 0.211 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.195 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 40.642α = 90
b = 42.791β = 113.67
c = 43.684γ = 90
Software Package:
Software NamePurpose
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling
SOLVEphasing
XTALVIEWrefinement

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2005-04-19
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance