1gor
From Proteopedia
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THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS-XYLOBIOSE COMPLEX AT 100 K
Overview
The substrate specificity of Thermoascus aurantiacus xylanase 10A (TAX), has been investigated both biochemically and structurally. High resolution, crystallographic analyses at 291 K and 100 K of TAX complexes with, xylobiose show that the ligand is in its alpha anomeric conformation and, provide a rationale for specificity on p-nitrophenyl glycosides at the -1, and -2 subsites. Trp 275, which is disordered in uncomplexed structures, is stabilised by its interaction with xylobiose. Two structural subsets in, family 10 are identified, which differ by the presence or absence of a, short helical stretch in the eighth betaalpha-loop of the TIM barrel, the, loop bearing Trp 275. This structural difference is discussed in the, context of Trp 275 mobility and xylanase function.
About this Structure
1GOR is a [Single protein] structure of sequence from [Thermoascus aurantiacus]. Active as [Endo-1,4-beta-xylanase], with EC number [3.2.1.8]. Structure known Active Site: ACI. Full crystallographic information is available from [OCA].
Reference
Substrate specificity and subsite mobility in T. aurantiacus xylanase 10A., Lo Leggio L, Kalogiannis S, Eckert K, Teixeira SC, Bhat MK, Andrei C, Pickersgill RW, Larsen S, FEBS Lett. 2001 Dec 7;509(2):303-8. PMID:11741607
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