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- Title
Correlation of temperature induced conformation change with optimum catalytic activity in the recombinant G/11 xylanase A from Bacillus subtilis strain 168 (1A1)
- Authors
Murakami, Mário T.; Arni, Raghuvir K.; Vieira, Davi S.; Degrève, Léo; Ruller, Roberto; Ward, Richard J.
- Abstract
Abstract: The 1.7Å resolution crystal structure of recombinant family G/11 β-1,4-xylanase (rXynA) from Bacillus subtilis 1A1 shows a jellyroll fold in which two curved β-sheets form the active-site and substrate-binding cleft. The onset of thermal denaturation of rXynA occurs at 328K, in excellent agreement with the optimum catalytic temperature. Molecular dynamics simulations at temperatures of 298–328K demonstrate that below the optimum temperature the thumb loop and palm domain adopt a closed conformation. However, at 328K these two domains separate facilitating substrate access to the active-site pocket, thereby accounting for the optimum catalytic temperature of the rXynA.
- Subjects
XYLANASES; BACILLUS subtilis; MOLECULAR dynamics; CATALYSIS
- Publication
FEBS Letters, 2005, Vol 579, Issue 28, p6505
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2005.10.039