1hiz
From Proteopedia
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XYLANASE T6 (XT6) FROM BACILLUS STEAROTHERMOPHILUS
Overview
Xylanases are hemicellulases that hydrolyze the internal, beta-1,4-glycoside bonds of xylan. The extracellular thermostable, endo-1,4-beta-xylanase (EC 3.2.1.8; XT6) produced by the thermophilic, bacterium Geobacillus stearothermophilus T-6 was shown to bleach pulp, optimally at pH 9 and 338 K and was successfully used in a large-scale, biobleaching mill trial. The xylanase gene was cloned and sequenced. The, mature enzyme consists of 379 amino acids, with a calculated molecular, weight of 43 808 Da and a pI of 9.0. Crystallographic studies of XT6 were, performed in order to study the mechanism of catalysis and to provide a, structural basis for the rational introduction of enhanced thermostability, by site-specific mutagenesis. XT6 was crystallized in the primitive, trigonal space group ... [(full description)]
About this Structure
1HIZ is a [Single protein] structure of sequence from [Geobacillus stearothermophilus] with GLA, GLC and SO4 as [ligands]. Active as [Endo-1,4-beta-xylanase], with EC number [3.2.1.8]. Structure known Active Site: GL1. Full crystallographic information is available from [OCA].
Reference
Structure determination of the extracellular xylanase from Geobacillus stearothermophilus by selenomethionyl MAD phasing., Teplitsky A, Mechaly A, Stojanoff V, Sainz G, Golan G, Feinberg H, Gilboa R, Reiland V, Zolotnitsky G, Shallom D, Thompson A, Shoham Y, Shoham G, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):836-48. Epub 2004, Apr 21. PMID:15103129
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