1gok
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The substrate specificity of Thermoascus aurantiacus xylanase 10A (TAX) | + | 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== | ==About this Structure== | ||
| - | 1GOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus]. This structure | + | 1GOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus]. This structure supersedes the now removed PDB entry 1TAX. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Known structural/functional Site: <scene name='pdbsite=ACI:Catalytic+Nucleophile'>ACI</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermoascus aurantiacus]] | [[Category: Thermoascus aurantiacus]] | ||
| - | [[Category: Leggio, L | + | [[Category: Leggio, L Lo.]] |
| - | [[Category: Pickersgill, R | + | [[Category: Pickersgill, R W.]] |
[[Category: family 10]] | [[Category: family 10]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: xylanase]] | [[Category: xylanase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:17 2008'' |
Revision as of 10:52, 21 February 2008
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THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS-CRYSTAL FORM II
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
1GOK is a Single protein structure of sequence from Thermoascus aurantiacus. This structure supersedes the now removed PDB entry 1TAX. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Known structural/functional Site: . 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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