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Mechanisms of Selectivity in Channels and Enzymes Studied with Interactive Molecular Dynamics

Identifieur interne : 000982 ( Pmc/Corpus ); précédent : 000981; suivant : 000983

Mechanisms of Selectivity in Channels and Enzymes Studied with Interactive Molecular Dynamics

Auteurs : Paul Grayson ; Emad Tajkhorshid ; Klaus Schulten

Source :

RBID : PMC:1303063

Abstract

Interactive molecular dynamics, a new modeling tool for rapid investigation of the physical mechanisms of biological processes at the atomic level, is applied to study selectivity and regulation of the membrane channel protein GlpF and the enzyme glycerol kinase. These proteins facilitate the first two steps of Escherichia coli glycerol metabolism. Despite their different function and architecture the proteins are found to employ common mechanisms for substrate selectivity: an induced geometrical fit by structurally homologous binding sites and an induced rapid dipole moment reversal. Competition for hydrogen bonding sites with water in both proteins is critical for substrate motion. In glycerol kinase, it is shown that the proposed domain motion prevents competition with water, in turn regulating the binding of glycerol.


Url:
PubMed: 12829462
PubMed Central: 1303063

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