3U7B

A new crystal structure of a Fusarium oxysporum GH10 xylanase reveals the presence of an extended loop on top of the catalytic cleft

3U7B の概要

• エントリーDOI: 10.2210/pdb3u7b/pdb
• 分子名称: ENDO-1,4-BETA-XYLANASE, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: tim barrel, xylanase, hydrolase
• 由来する生物種: Fusarium oxysporum
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 186383.30

構造登録者

Dimarogona, M.,Topakas, E.,Christakopoulos, P.,Chrysina, E.D. (登録日: 2011-10-13, 公開日: 2012-07-18, 最終更新日: 2024-11-06)

主引用文献

Dimarogona, M.,Topakas, E.,Christakopoulos, P.,Chrysina, E.D.
The structure of a GH10 xylanase from Fusarium oxysporum reveals the presence of an extended loop on top of the catalytic cleft.
Acta Crystallogr.,Sect.D, 68:735-742, 2012

PubMed 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 P4(1)2(1)2 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 α6 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.

PubMed: 22751658
DOI: 10.1107/S0907444912007044

実験手法

X-RAY DIFFRACTION (1.94 Å)