|
A. V. Popinako, M. Yu. Antonov, E. Yu. Bezsudnova, V. O. Popov
The role of
charged residues in the structural adaptation of short-chain
alcohldehydrogenase (SDR) from thermophilic organisms to high temperatures
Abstract
Understanding
the adaptation mechanisms of proteins from extremophiles paves the way for
development of new biocatalysts resistant to extreme proton deficit. In the
present work, we study the structural adaptation of NADP-dependent short-chain
alcohol dehydrogenases SDR (Short-chain Dehydrogenase/Reductase) to high
temperatures. In this paper we present the results of the analysis of the
amino acid composition of the SDR sequences, the results of the comparative
analysis of the structural elements of the SDR from mesophiles and
thermophiles, as well as the results of the molecular dynamics of the superthermostable
short-chain alcohol dehydrogenase from the hyperthermophilic
archaeon Thermococcus sibiricus (TsAdh319) and its homologues.
Key words:
modeling, structural adaptation, thermophils, mesophiles.
Copyright (C) Chemistry Dept., Moscow State University, 2002
|
|
