dc.contributor | Universidade Estadual Paulista (Unesp) | |
dc.contributor | Universidade de São Paulo (USP) | |
dc.date.accessioned | 2014-05-20T14:02:21Z | |
dc.date.accessioned | 2022-10-05T14:50:12Z | |
dc.date.available | 2014-05-20T14:02:21Z | |
dc.date.available | 2022-10-05T14:50:12Z | |
dc.date.created | 2014-05-20T14:02:21Z | |
dc.date.issued | 2005-11-21 | |
dc.identifier | Febs Letters. Amsterdam: Elsevier B.V., v. 579, n. 28, p. 6505-6510, 2005. | |
dc.identifier | 0014-5793 | |
dc.identifier | http://hdl.handle.net/11449/21972 | |
dc.identifier | 10.1016/j.febslet.2005.10.039 | |
dc.identifier | WOS:000233520700034 | |
dc.identifier | WOS000233520700034.pdf | |
dc.identifier | 9162508978945887 | |
dc.identifier | 0000-0003-2460-1145 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/3895666 | |
dc.description.abstract | 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. | |
dc.language | eng | |
dc.publisher | Elsevier B.V. | |
dc.relation | FEBS Letters | |
dc.relation | 1,991 | |
dc.rights | Acesso aberto | |
dc.source | Web of Science | |
dc.subject | thermostable enzyme | |
dc.subject | Crystal structure | |
dc.subject | molecular dynamics | |
dc.title | Correlation of temperature induced conformation change with optimum catalytic activity in the recombinant G/11 xylanase A from Bacillus subtilis strain 168 (1A1) | |
dc.type | Artigo | |