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M. Vas, A. Varga, J. Szabo, E. Graczer, B. Flachner, P. Zavodszky, P. Konarev, D. Svergun
Insight into the mechanism of domain movements and its role
in functioning of 3-phosphoglycerate kinase
Abstract
Comprehensive studies with 3-phosphoglycerate kinase
revealed the details of transmission of substrate triggered conformational
effect towards the main molecular hinge at the b-strand L. The unusual kinetic
behaviour (activation by anions) and flexibility of the phosphate chain of the
nucleotide substrate(s) can be related to domain movements. Both phenomena are
due to the interactions with the catalytic Lys residue, which moves more than
10 E during domain closure. This
movement occurs, in concert with operation of the main hinge, under the
simultaneous action of the two substrates.
Copyright (C) Chemistry Dept., Moscow State University, 2002
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