1IIB

CRYSTAL STRUCTURE OF IIBCELLOBIOSE FROM ESCHERICHIA COLI


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.241 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.187 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases.

van Montfort, R.L.Pijning, T.Kalk, K.H.Reizer, J.Saier Jr., M.H.Thunnissen, M.M.Robillard, G.T.Dijkstra, B.W.

(1997) Structure 5: 217-225

  • DOI: https://doi.org/10.1016/s0969-2126(97)00180-9
  • Primary Citation of Related Structures:  
    1IIB

  • PubMed Abstract: 

    . The bacterial phosphoenolpyruvate-dependent phosphotransferase system (PTS) mediates the energy-driven uptake of carbohydrates and their concomitant phosphorylation. In addition, the PTS is intimately involved in the regulation of a variety of metabolic and transcriptional processes in the bacterium. The multiprotein PTS consists of a membrane channel and at least four cytoplasmic proteins or protein domains that sequentially transfer a phosphoryl group from phosphoenolpyruvate to the transported carbohydrate. Determination of the three-dimensional structure of the IIB enzymes within the multiprotein complex would provide insights into the mechanisms by which they promote efficient transport by the membrane channel IIC protein and phosphorylate the transported carbohydrate on the inside of the cell.


  • Organizational Affiliation

    Laboratory of Biophysical Chemistry, Biochemistry and BIOSON Research Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen The Netherlands.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ENZYME IIB OF THE CELLOBIOSE-SPECIFIC PHOSPHOTRANSFERASE SYSTEM
A, B
106Escherichia coli K-12Mutation(s): 1 
Gene Names: CELA
EC: 2.7.1.69
UniProt
Find proteins for P69795 (Escherichia coli (strain K12))
Explore P69795 
Go to UniProtKB:  P69795
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP69795
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.241 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.187 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 53.791α = 90
b = 31.782β = 101.7
c = 60.253γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
XDSdata reduction
BIOMOLdata scaling
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1997-12-24
    Type: Initial release
  • Version 1.1: 2008-03-05
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.3: 2021-11-03
    Changes: Data collection, Database references, Other
  • Version 1.4: 2024-02-07
    Changes: Data collection