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.
Structure of the UreD–UreF–UreG–UreE complex in Helicobacter pylori: a model study / Francesco Biagi; Francesco Musiani; Stefano Ciurli. - In: JBIC. - ISSN 0949-8257. - STAMPA. - 18:(2013), pp. 571-577. [10.1007/s00775-013-1002-8]
Structure of the UreD–UreF–UreG–UreE complex in Helicobacter pylori: a model study
MUSIANI, FRANCESCO;CIURLI, STEFANO LUCIANO
2013
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
