Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/167831
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Structural analysis of glucuronoxylan-specific Xyn30D and its attached CBM35 domain gives insights into the role of modularity in specificity |
Autor: | Sainz-Polo, M. Ángela CSIC; Valenzuela, S.V.; González, Beatriz CSIC ORCID; Pastor, F. I. Javier; Sanz-Aparicio, J. CSIC ORCID | Fecha de publicación: | 2014 | Editor: | American Society for Biochemistry and Molecular Biology | Citación: | Journal of Biological Chemistry 289: 31088- 31101 (2014) | Resumen: | © 2014 by The American Society for Biochemistry and Molecular Biology Inc. Glucuronoxylanase Xyn30D is a modular enzyme containing a family 30 glycoside hydrolase catalytic domain and an attached carbohydrate binding module of the CBM35 family.Wepresent here the three-dimensional structure of the full-length Xyn30D at 2.4 Å resolution. The catalytic domain folds into an (α/β)8 barrel with an associated β-structure, whereas the attached CBM35 displays a jellyroll β-sandwich including two calcium ions. Although both domains fold in an independent manner, the linker region makes polar interactions with the catalytic domain, allowing a moderate flexibility. The ancillary Xyn30DCBM35 domain has been expressed and crystallized, and its binding abilities have been investigated by soaking experiments. Only glucuronic acid-containing ligands produced complexes, and their structures have been solved. A calcium-dependent glucuronic acid binding site shows distinctive structural features as compared with other uronic acid-specific CBM35s, because the presence of two aromatic residues delineates a wider pocket. The nonconserved Glu129 makes a bidentate link to calcium and defines region E, previously identified as specificity hot spot. The molecular surface of Xyn30D-CBM35 shows a unique stretch of negative charge distribution extending from its binding pocket that might indicate some oriented interaction with its target substrate. The binding ability of Xyn30D-CBM35 to different xylans was analyzed by affinity gel electrophoresis. Some binding was observed with rye glucuronoarabinoxylan in presence of calcium chelating EDTA, which would indicate that Xyn30D-CBM35 might establish interaction to other components of xylan, such as arabinose decorations of glucuronoarabinoxylan. A role in depolymerization of highly substituted chemically complex xylans is proposed. | URI: | http://hdl.handle.net/10261/167831 | DOI: | 10.1074/jbc.M114.597732 | Identificadores: | doi: 10.1074/jbc.M114.597732 issn: 1083-351X |
Aparece en las colecciones: | (IQF) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
13
checked on 04-abr-2024
SCOPUSTM
Citations
31
checked on 11-abr-2024
WEB OF SCIENCETM
Citations
29
checked on 25-feb-2024
Page view(s)
254
checked on 18-abr-2024
Download(s)
98
checked on 18-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
Artículos relacionados:
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.