1k6a: Difference between revisions

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[[Image:1k6a.~~gif~~|left|200px]]

[[Image:1k6a.png|left|200px]]

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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.

==About this Structure==

1K6A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1fxm 1fxm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6A 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:[http://www.ncbi.nlm.nih.gov/pubmed/11741607 11741607]

[[Category: Endo-1,4-beta-xylanase]]

[[Category: Single protein]]

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[[Category: Active site mobility]]

[[Category: Alternate conformation]]

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-[[Image:1k6a.gif|left|200px]]
+[[Image:1k6a.png|left|200px]]
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-==Overview==
+{{ABSTRACT_11741607}}
-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==
 K6A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1fxm 1fxm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6A 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:[http://www.ncbi.nlm.nih.gov/pubmed/11741607 11741607]
 [[Category: Endo-1,4-beta-xylanase]]
 [[Category: Single protein]]
@@ Line 33: / Line 29: @@
 [[Category: Active site mobility]]
 [[Category: Alternate conformation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:21:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 25 19:17:27 2008''