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DC Field | Value | Language |
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dc.contributor.author | Murakami, M. T. | - |
dc.contributor.author | Arni, R. K. | - |
dc.contributor.author | Vieira, D. S. | - |
dc.contributor.author | Degreve, L. | - |
dc.contributor.author | Ruller, R. | - |
dc.contributor.author | Ward, R. J. | - |
dc.date.accessioned | 2014-05-20T14:02:21Z | - |
dc.date.available | 2014-05-20T14:02:21Z | - |
dc.date.issued | 2005-11-21 | - |
dc.identifier | http://dx.doi.org/10.1016/j.febslet.2005.10.039 | - |
dc.identifier.citation | Febs Letters. Amsterdam: Elsevier B.V., v. 579, n. 28, p. 6505-6510, 2005. | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | http://hdl.handle.net/11449/21972 | - |
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. | en |
dc.format.extent | 6505-6510 | - |
dc.language.iso | eng | - |
dc.publisher | Elsevier B.V. | - |
dc.source | Web of Science | - |
dc.subject | thermostable enzyme | pt |
dc.subject | Crystal structure | pt |
dc.subject | molecular dynamics | pt |
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) | en |
dc.type | outro | - |
dc.contributor.institution | Universidade Estadual Paulista (UNESP) | - |
dc.contributor.institution | Universidade de São Paulo (USP) | - |
dc.description.affiliation | UNESP, IBILCE, Dept Phys, São Paulo, Brazil | - |
dc.description.affiliation | Univ São Paulo, FMRP, Dept Cellular & Mol Biol, BR-14049 Ribeirao Preto, SP, Brazil | - |
dc.description.affiliation | Univ São Paulo, FFCLRP, Dept Chem, BR-14049 Ribeirao Preto, SP, Brazil | - |
dc.description.affiliationUnesp | UNESP, IBILCE, Dept Phys, São Paulo, Brazil | - |
dc.identifier.doi | 10.1016/j.febslet.2005.10.039 | - |
dc.identifier.wos | WOS:000233520700034 | - |
dc.rights.accessRights | Acesso aberto | - |
dc.identifier.file | WOS000233520700034.pdf | - |
dc.relation.ispartof | FEBS Letters | - |
Appears in Collections: | Artigos, TCCs, Teses e Dissertações da Unesp |
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