| Literature DB >> 24530907 |
J Domingo Meza-Aguilar1, Petra Fromme2, Alfredo Torres-Larios3, Guillermo Mendoza-Hernández4, Ulises Hernandez-Chiñas1, Roberto A Arreguin-Espinosa de Los Monteros4, Carlos A Eslava Campos1, Raimund Fromme5.
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.Entities:
Keywords: 4OM9; Autotransporter; EAEC; Passenger domain; Plasmid encoded toxin(Pet); SPATE
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Year: 2014 PMID: 24530907 PMCID: PMC4005925 DOI: 10.1016/j.bbrc.2014.02.016
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575