The structure of a GH10 xylanase from Fusarium oxysporum reveals the presence of an extended loop on top of the catalytic cleft

Dimarogona, M; Topakas, E; Christakopoulos, P; Chrysina, ED

dc.contributor.author	Dimarogona, M	en
dc.contributor.author	Topakas, E	en
dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Chrysina, ED	en
dc.date.accessioned	2014-03-01T02:14:50Z
dc.date.available	2014-03-01T02:14:50Z
dc.date.issued	2012	en
dc.identifier.issn	09074449	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/30140
dc.subject	biocatalysts	en
dc.subject	Fusarium oxysporum	en
dc.subject	GH10 xylanases	en
dc.title	The structure of a GH10 xylanase from Fusarium oxysporum reveals the presence of an extended loop on top of the catalytic cleft	en
heal.type	journalArticle	en
heal.identifier.primary	10.1107/S0907444912007044	en
heal.identifier.secondary	http://dx.doi.org/10.1107/S0907444912007044	en
heal.publicationDate	2012	en
heal.abstract	Xylanase enzymes have been the focus of considerable research in recent decades owing to their extensive use in a variety of biotechnological applications. Previous structural studies of a number of GH10 xylanases revealed that all GH10 family members have the (β/α)8-barrel fold and their catalytic site is conserved. The structure of a new GH10 xylanase from Fusarium oxysporum (FoXyn10a) was determined at 1.94 Å resolution from crystals belonging to the tetragonal space group P41212 with five molecules per asymmetric unit. Comparison of the structure of FoXyn10a with previously determined structures of GH10 family members indicated that most of the differences were located in the loop regions between the ordered secondary-structure elements of the barrel, as expected. However, alignment of FoXyn10a with sequence and structural homologues denoted an atypically long loop connecting strand β6b and helix 6 that was only present in one other GH10 xylanase, the structure of which is not known. This structural feature may be of functional importance, with potential implications in the catalytic efficiency of the enzyme. © 2012 International Union of Crystallography. Printed in Singapore - all rights reserved.	en
heal.journalName	Acta Crystallographica Section D: Biological Crystallography	en
dc.identifier.doi	10.1107/S0907444912007044	en
dc.identifier.volume	68	en
dc.identifier.issue	7	en
dc.identifier.spage	735	en
dc.identifier.epage	742	en