title: Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: a model study.
abstract: The molecular details of the protein complex formed by UreD, UreF, UreG, and UreE, accessory proteins for urease activation in the carcinogenic bacterium Helicobacter pylori, have been elucidated using computational modeling. The calculated structure of the complex supports the hypothesis of UreF acting as a GTPase activation protein that facilitates GTP hydrolysis by UreG during urease maturation, and provides a rationale for the design of new drugs against infections by ureolytic bacterial pathogens.
authors: Laboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology, University of Bologna, Bologna, Italy.
authors: Francesco
authors: F
authors: Biagi
authors: Francesco
authors: F
authors: Musiani
authors: Stefano
authors: S
authors: Ciurli
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D016480:Helicobacter pylori / Q000201:enzymology / Q000378:metabolism*; D028044:Phosphate-Binding Proteins; D017433:Protein Structure, Secondary; D014510:Urease / Q000737:chemistry / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D028044:Phosphate-Binding Proteins; C086767:UreD protein, Bacteria; C090404:UreE protein, Bacteria; C101639:UreF protein, bacteria; C082270:ureG protein, Bacteria; D014510:Urease
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