期刊
FEBS LETTERS
卷 579, 期 28, 页码 6505-6510出版社
WILEY
DOI: 10.1016/j.febslet.2005.10.039
关键词
thermostable enzyme; crystal structure; molecular dynamics
资金
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [03/01457-2] Funding Source: FAPESP
The 1.7 angstrom resolution crystal structure of recombinant family G/11 beta-1,4-xylanase (rXynA) from Bacillus subtilis 1A1 shows a jellyroll fold in which two curved P-sheets form the active-site and substrate-binding cleft. The onset of thermal denaturation of rXynA occurs at 328 K, in excellent agreement with the optimum catalytic temperature. Molecular dynamics simulations at temperatures of 298-328 K demonstrate that below the optimum temperature the thumb loop and palm domain adopt a closed conformation. However, at 328 K these two domains separate facilitating substrate access to the active-site pocket, thereby accounting for the optimum catalytic temperature of the rXynA. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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