4OM9 : X-Ray Crystal Structure of the passenger domain of Plasmid encoded toxin, an Autrotansporter Enterotoxin from enteroaggregative Escherichia coli (EAEC)

  • Raimund Fromme (Contributor)
  • Petra Fromme (Contributor)
  • J. Domingo Meza-Aguilar (Contributor)
  • Alfredo Torres-Larios (Contributor)
  • Ulises Hernandez-Chiñas (Contributor)
  • Carlos A. Eslava Campos (Contributor)
  • Guillermo Mendoza-Hernández (Contributor)
  • Roberto A. Arreguin-Espinosa De Los Monteros (Contributor)

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.3
Classification:HYDROLASE
Release Date:2014-03-12
Deposition Date:2014-01-27
Revision Date:2014-03-26#2014-04-02
Molecular Weight:104055.56
Macromolecule Type:Protein
Residue Count:966
Atom Site Count:7043
DOI:10.2210/pdb4om9/pdb

Abstract:
Autotransporters (ATs) represent a superfamily of proteins produced by a variety of pathogenic bacteria, which include the pathogenic groups of Escherichia coli (E. coli) associated with gastrointestinal and urinary tract infections. We present the first X-ray structure of the passenger domain from the Plasmid-encoded toxin (Pet) a 100 kDa protein at 2.3 Å resolution which is a cause of acute diarrhea in both developing and industrialized countries. Pet is a cytoskeleton-altering toxin that induces loss of actin stress fibers. While Pet (pdb code: 4OM9) shows only a sequence identity of 50% compared to the closest related protein sequence, extracellular serine protease plasmid (EspP) the structural features of both proteins are conserved. A closer structural look reveals that Pet contains a β-pleaded sheet at the sequence region of residues 181-190, the corresponding structural domain in EspP consists of a coiled loop. Secondary, the Pet passenger domain features a more pronounced beta sheet between residues 135 and 143 compared to the structure of EspP.
Date made availableMar 12 2014
PublisherRCSB-PDB

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