1NQ6

Crystal Structure of the catalytic domain of xylanase A from Streptomyces halstedii JM8

1NQ6 の概要

• エントリーDOI: 10.2210/pdb1nq6/pdb
• 分子名称: Xys1, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: glycoside hydrolase family 10, xylanase, xylan degradation, hydrolase
• 由来する生物種: Streptomyces halstedii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32638.38

構造登録者

Canals, A.,Vega, M.C.,Gomis-Ruth, F.X.,Santamaria, R.I.,Coll, M. (登録日: 2003-01-21, 公開日: 2004-01-21, 最終更新日: 2024-11-13)

主引用文献

Canals, A.,Vega, M.C.,Gomis-Ruth, F.X.,Diaz, M.,Santamaria R, R.I.,Coll, M.
Structure of xylanase Xys1delta from Streptomyces halstedii.
Acta Crystallogr.,Sect.D, 59:1447-1453, 2003

PubMed Abstract: Xylanases hydrolyze the beta-1,4-linked xylose backbone of xylans. They are of increasing interest in the paper and food industries for their pre-bleaching and bio-pulping applications. Such industries demand new xylanases to cover a wider range of cleavage specificity, activity and stability. The catalytic domain of xylanase Xys1 from Streptomyces halstedii JM8 was expressed, purified and crystallized and native data were collected to 1.78 A resolution with an R(merge) of 4.4%. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.05, b = 79.60, c = 87.80 A. The structure was solved by the molecular-replacement method using the structure of the homologue Xyl10A from Streptomyces lividans. In a similar manner to other members of its family, Xys1 folds to form a standard (beta/alpha)(8) barrel with the two catalytic functions, the acid/base and the nucleophile, at its C-terminal side. The overall structure is described and compared with those of related xylanases.

PubMed: 12876348
DOI: 10.1107/S0907444903012629

実験手法

X-RAY DIFFRACTION (1.78 Å)