1k6a
From Proteopedia
(New page: 200px<br /><applet load="1k6a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k6a, resolution 1.14Å" /> '''Structural studies o...) |
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| - | [[Image:1k6a.gif|left|200px]]<br /><applet load="1k6a" size=" | + | [[Image:1k6a.gif|left|200px]]<br /><applet load="1k6a" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k6a, resolution 1.14Å" /> | caption="1k6a, resolution 1.14Å" /> | ||
'''Structural studies on the mobility in the active site of the Thermoascus aurantiacus xylanase I'''<br /> | '''Structural studies on the mobility in the active site of the Thermoascus aurantiacus xylanase I'''<br /> | ||
==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== | ||
| - | 1K6A 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 | + | 1K6A 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 1FXM. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6A OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Thermoascus aurantiacus]] | [[Category: Thermoascus aurantiacus]] | ||
[[Category: Andrei, C.]] | [[Category: Andrei, C.]] | ||
| - | [[Category: Bhat, M | + | [[Category: Bhat, M K.]] |
[[Category: Eckert, K.]] | [[Category: Eckert, K.]] | ||
[[Category: Kalogiannis, S.]] | [[Category: Kalogiannis, S.]] | ||
[[Category: Larsen, S.]] | [[Category: Larsen, S.]] | ||
| - | [[Category: Leggio, L | + | [[Category: Leggio, L Lo.]] |
| - | [[Category: Pickersgill, R | + | [[Category: Pickersgill, R W.]] |
| - | [[Category: Teixeira, S | + | [[Category: Teixeira, S C.M.]] |
[[Category: active site mobility]] | [[Category: active site mobility]] | ||
[[Category: alternate conformations]] | [[Category: alternate conformations]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:35 2008'' |
Revision as of 11:30, 21 February 2008
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Structural studies on the mobility in the active site of the Thermoascus aurantiacus xylanase I
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
1K6A is a Single protein structure of sequence from Thermoascus aurantiacus. This structure supersedes the now removed PDB entry 1FXM. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 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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