X-ray crystal structure of the passenger domain of plasmid encoded toxin(Pet), an autotransporter enterotoxin from enteroaggregative Escherichia coli (EAEC)

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• 作者：J. Domingo Meza-Aguilar^a ; ^b ; Petra Fromme^c ; Alfredo Torres-Larios^d ; Guillermo Mendoza-Herná ; ndez^e ; Ulises Hernandez-Chiñ ; as^a ; ^b ; Roberto A. Arreguin-Espinosa de los Monteros^e ; Carlos A. Eslava Campos^a ; ^b ; ; Raimund Fromme^c ; ^{Raimund.Fromme@asu.edu" class="auth_mail}
• 关键词：Plasmid encoded toxin(Pet) ; Passenger domain ; Autotransporter ; 4OM9 ; EAEC ; SPATE
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：7 March, 2014
• 年：2014
• 卷：445
• 期：2
• 页码：439-444
• 全文大小：1300 K

文摘

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 脜 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 尾-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.