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Crystallization and preliminary X‐ray diffraction analysis of Xyn30D from Paenibacillus barcinonensis
Author(s) -
SainzPolo María Ángela,
Valenzuela Susana Valeria,
Pastor F. Javier,
SanzAparicio Julia
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14012035
Subject(s) - glycoside hydrolase , chemistry , glucuronate , xylanase , hydrolysis , depolymerization , enzyme , xylan , stereochemistry , hydrolase , immobilized enzyme , biochemistry , organic chemistry
Xyn30D, a new member of a recently identified group of xylanases, has been purified and crystallized. Xyn30D is a bimodular enzyme composed of an N‐terminal catalytic domain belonging to glycoside hydrolase family 30 (GH30) and a C‐terminal family 35 carbohydrate‐binding domain (CBM35) able to bind xylans and glucuronic acid. Xyn30D shares the characteristic endo mode of action described for GH30 xylanases, with the hydrolysis of the β‐(1,4) bonds of xylan being directed by α‐1,2‐linked glucuronate moieties, which have to be placed at the −2 subsite of the xylanase active site. Crystals of the complete enzyme were obtained and a full data set to 2.3 Å resolution was collected using a synchrotron X‐ray source. This represents the first bimodular enzyme with the domain architecture GH30‐CBM35. This study will contribute to the understanding of the role that the different xylanases play in the depolymerization of glucuronoxylan.