1gom: Difference between revisions

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[[Image:1gom.~~gif~~|left|200px]]

[[Image:1gom.png|left|200px]]

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~~'''~~THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS-CRYSTAL FORM I~~'''~~

===THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS-CRYSTAL FORM I===

~~==Overview==~~

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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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_11741607}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11741607 is the PubMed ID number.

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==About this Structure==

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[[Category: Plant cell wall degradation]]

[[Category: Xylanase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 17~~:49:40 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:36:40 2008''

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-[[Image:1gom.gif|left|200px]]
+{{Seed}}
+[[Image:1gom.png|left|200px]]
 <!--
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 {{STRUCTURE_1gom|  PDB=1gom  |  SCENE=  }}
-'''THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS-CRYSTAL FORM I'''
+===THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS-CRYSTAL FORM 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11741607}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11741607 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11741607}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Plant cell wall degradation]]
 [[Category: Xylanase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:49:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 05:36:40 2008''