1gor: Difference between revisions

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==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 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==

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[[Category: Thermoascus aurantiacus]]

[[Category: Larsen, S.]]

[[Category: Leggio, L.Lo.]]

[[Category: Leggio, L Lo.]]

[[Category: family 10]]

[[Category: hydrolase]]

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[[Category: xylanase]]

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@@ Line 4: / Line 4: @@
 ==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 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==
@@ Line 15: / Line 15: @@
 [[Category: Thermoascus aurantiacus]]
 [[Category: Larsen, S.]]
-[[Category: Leggio, L.Lo.]]
+[[Category: Leggio, L Lo.]]
 [[Category: family 10]]
 [[Category: hydrolase]]
@@ Line 22: / Line 22: @@
 [[Category: xylanase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:41:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:20 2008''