Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051810 | FEBS Letters | 2005 | 6 Pages |
Abstract
The 1.7 Å 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 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.
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Authors
Mário T. Murakami, Raghuvir K. Arni, Davi S. Vieira, Léo Degrève, Roberto Ruller, Richard J. Ward,