1w3h

From Proteopedia

Revision as of 14:19, 30 October 2007

THE 3-DIMENSIONAL STRUCTURE OF A THERMOSTABLE MUTANT OF A XYLANASE (XYN10A) FROM CELLVIBRIO JAPONICUS

Overview

Metal ions such as calcium often play a key role in protein, thermostability. The inclusion of metal ions in industrial processes is, however, problematic. Thus, the evolution of enzymes that display enhanced, stability, which is not reliant on divalent metals, is an important, biotechnological goal. Here we have used forced protein evolution to, interrogate whether the stabilizing effect of calcium in an industrially, relevant enzyme can be replaced with amino acid substitutions. Our study, has focused on the GH10 xylanase CjXyn10A from Cellvibrio japonicus, which, contains an extended calcium binding loop that confers proteinase, resistance and thermostability. Three rounds of error-prone PCR and, selection identified a treble mutant, D262N/A80T/R347C, which in the, absence of calcium ... [(full description)]

About this Structure

1W3H is a [Single protein] structure of sequence from [Cellvibrio japonicus] with CA and EDO as [ligands]. Active as [Endo-1,4-beta-xylanase], with EC number [3.2.1.8]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The use of forced protein evolution to investigate and improve stability of family 10 xylanases. The production of Ca2+-independent stable xylanases., Andrews SR, Taylor EJ, Pell G, Vincent F, Ducros VM, Davies GJ, Lakey JH, Gilbert HJ, J Biol Chem. 2004 Dec 24;279(52):54369-79. Epub 2004 Sep 27. PMID:15452124

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