Crystal structure of CagZ, a protein from the Helicobacter pylori pathogenicity island that encodes for a type IV secretion system

Journal of Molecular Biology
Laura CendronGiuseppe Zanotti

Abstract

CagZ, a 23 kDa protein encoded by the cagZ gene (HP0526) of the cag pathogenicity island of Helicobacter pylori, has been cloned, over-expressed, purified and its three-dimensional structure determined. The protein consists of a single compact L-shaped domain, composed of seven alpha-helices including about 70% of the total residues. Three-dimensional homology searches did not reveal structural homologues, and CagZ can be considered representative of a new protein fold. The presence of a disordered C-terminal tail and the nature of the molecular surface suggest that CagZ may participate in the interaction of effector proteins with one or more components of the H.pylori type IV secretion system on the cytoplasmic side of the inner membrane.

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Citations

Jun 22, 2006·Journal of Bacteriology·Valerie J BuslerTimothy L Cover
Nov 3, 2011·Cell Communication and Signaling : CCS·Steffen BackertNicole Tegtmeyer
Feb 13, 2016·Cellular and Molecular Life Sciences : CMLS·Andrea VanniniAlberto Danielli
Jul 12, 2007·Proteins·Laura CendronGiuseppe Zanotti
Mar 1, 2011·The FEBS Journal·Laurent Terradot, Gabriel Waksman
Jun 4, 2015·Annual Review of Biochemistry·Vidya Chandran Darbari, Gabriel Waksman
May 5, 2017·The FEBS Journal·Enrique MerinoGermán Rubén Aguilar-Gutiérrez
Jun 6, 2015·American Journal of Physiology. Gastrointestinal and Liver Physiology·Charles E HammondAdam J Smolka

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