Structure of xylanase Xys1Δ from Streptomyces halstedii

Xylanases hydrolyze the β‐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 cata...

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Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2003-08, Vol.59 (8), p.1447-1453
Main Authors: Canals, Albert, Vega, M. Cristina, Gomis-Rüth, F. Xavier, Díaz, Margarita, Santamaría, Ramón I., Coll, Miquel
Format: Article
Language:English
Subjects:
glycoside hydrolase family 10
TIM-barrel fold
xylan degradation
xylanases
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container_issue 8
container_start_page 1447
container_title Acta crystallographica. Section D, Biological crystallography.
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creator Canals, Albert
Vega, M. Cristina
Gomis-Rüth, F. Xavier
Díaz, Margarita
Santamaría, Ramón I.
Coll, Miquel
description Xylanases hydrolyze the β‐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 Å resolution with an Rmerge of 4.4%. The crystals belong to space group P212121, with unit‐cell parameters a = 34.05, b = 79.60, c = 87.80 Å. 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 (β/α)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.
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source Wiley-Blackwell Read & Publish Collection; Alma/SFX Local Collection
subjects glycoside hydrolase family 10
TIM-barrel fold
xylan degradation
xylanases
title Structure of xylanase Xys1Δ from Streptomyces halstedii
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