4om9
From Proteopedia
X-Ray Crystal Structure of the passenger domain of Plasmid encoded toxin, an Autrotansporter Enterotoxin from enteroaggregative Escherichia coli (EAEC)
Structural highlights
FunctionPET_ECO44 Serine protease with enterotoxic and cytotoxic activity. Internalization into the host cell is required for the induction of cytopathic effects. However, the serine activity is not necessary for secretion and internalization into the host cell.[1] [2] [3] [4] Publication Abstract from PubMedAutotransporters (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 100kDa protein at 2.3A 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 beta-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. X-ray crystal structure of the passenger domain of plasmid encoded toxin(Pet), an autotransporter enterotoxin from enteroaggregative Escherichia coli (EAEC).,Domingo Meza-Aguilar J, Fromme P, Torres-Larios A, Mendoza-Hernandez G, Hernandez-Chinas U, Arreguin-Espinosa de Los Monteros RA, Eslava Campos CA, Fromme R Biochem Biophys Res Commun. 2014 Feb 12. pii: S0006-291X(14)00268-X. doi:, 10.1016/j.bbrc.2014.02.016. PMID:24530907[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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