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Structural and molecular mechanism for autoprocessing of MARTX toxin of Vibrio cholerae at multiple sites

SYSNO ASEP	0336360
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Structural and molecular mechanism for autoprocessing of MARTX toxin of Vibrio cholerae at multiple sites
Author(s)	Procházková, K. (US) Shuvalova, L. A. (US) Minasov, G. (US) Voburka, Zdeněk (UOCHB-X) Anderson, W. F. (US) Satchell, K. J. F. (US)
Number of authors	6
Source Title	Journal of Biological Chemistry. - : Elsevier - ISSN 0021-9258 Roč. 284, č. 39 (2009), s. 26557-26568
Number of pages	12 s.
Language	eng - English
Country	US - United States
Keywords	autoprocessing ; activator InsP6 inositol hexakisphosphate ; CPD cysteine protease domain ; MARTX(Vc)
Subject RIV	CE - Biochemistry
CEZ	AV0Z40550506 - UOCHB-X (2005-2011)
UT WOS	000269969600037
DOI	10.1074/jbc.M109.25510
Annotation	The multifunctional autoprocessing repeats-in-toxin (MARTX) toxin of Vibrio cholerae causes destruction of the actin cytoskeleton by covalent cross-linking of actin and inactivation of Rho GTPases. The effector domains responsible for these activities are here shown to be independent proteins released from the large toxin by autoproteolysis catalyzed by an embedded cysteine protease domain (CPD). The CPD is activated upon binding inositol hexakisphosphate (InsP6). In this study, we demonstrated that InsP6 is not simply an allosteric cofactor, but rather binding of InsP6 stabilized the CPD structure, facilitating formation of the enzyme-substrate complex.
Workplace	Institute of Organic Chemistry and Biochemistry
Contact	asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434
Year of Publishing	2010

Number of the records: 1