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

0336360 - ÚOCHB 2010 RIV US eng J - Článek v odborném periodiku
Procházková, K. - Shuvalova, L. A. - Minasov, G. - Voburka, Zdeněk - Anderson, W. F. - Satchell, K. J. F.
Structural and molecular mechanism for autoprocessing of MARTX toxin of Vibrio cholerae at multiple sites.
Journal of Biological Chemistry. Roč. 284, č. 39 (2009), s. 26557-26568. ISSN 0021-9258. E-ISSN 1083-351X
Výzkumný záměr: CEZ:AV0Z40550506
Klíčová slova: autoprocessing * activator InsP6 inositol hexakisphosphate * CPD cysteine protease domain * MARTX(Vc)
Kód oboru RIV: CE - Biochemie
Impakt faktor: 5.328, rok: 2009

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.
Trvalý link: http://hdl.handle.net/11104/0180609