X-ray crystal structure of the passenger domain of plasmid encoded toxin(Pet), an autotransporter enterotoxin from enteroaggregative Escherichia coli (EAEC)
2014; Elsevier BV; Volume: 445; Issue: 2 Linguagem: Inglês
10.1016/j.bbrc.2014.02.016
ISSN1090-2104
AutoresJ. Domingo Meza-Aguilar, Petra Fromme, Alfredo Torres‐Larios, Guillermo Mendoza‐Hernández, Ulises Hernández‐Chiñas, Roberto Arreguı́n-Espinosa, Carlos Alberto Eslava Campos, Raimund Fromme,
Tópico(s)Viral gastroenteritis research and epidemiology
ResumoAutotransporters (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.
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