1h4h
From Proteopedia
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| - | [[Image:1h4h.gif|left|200px]]<br /> | + | [[Image:1h4h.gif|left|200px]]<br /><applet load="1h4h" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1h4h" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1h4h, resolution 1.90Å" /> | caption="1h4h, resolution 1.90Å" /> | ||
'''OLIGOSACCHARIDE-BINDING TO FAMILY 11 XYLANASES: BOTH COVALENT INTERMEDIATE AND MUTANT-PRODUCT COMPLEXES DISPLAY 2,5B CONFORMATIONS AT THE ACTIVE-CENTRE'''<br /> | '''OLIGOSACCHARIDE-BINDING TO FAMILY 11 XYLANASES: BOTH COVALENT INTERMEDIATE AND MUTANT-PRODUCT COMPLEXES DISPLAY 2,5B CONFORMATIONS AT THE ACTIVE-CENTRE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H4H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_agaradhaerens Bacillus agaradhaerens]. 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] | + | 1H4H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_agaradhaerens Bacillus agaradhaerens]. 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=BC3:Xys Binding Site For Residue D1211'>BC3</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H4H OCA]. |
==Reference== | ==Reference== | ||
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[[Category: xylanase]] | [[Category: xylanase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:58:37 2007'' |
Revision as of 13:48, 18 December 2007
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OLIGOSACCHARIDE-BINDING TO FAMILY 11 XYLANASES: BOTH COVALENT INTERMEDIATE AND MUTANT-PRODUCT COMPLEXES DISPLAY 2,5B CONFORMATIONS AT THE ACTIVE-CENTRE
Overview
The glycoside hydrolase sequence-based classification reveals two families, of enzymes which hydrolyse the beta-1,4-linked backbone of xylan, xylanases, termed families GH-10 and GH-11. Family GH-11 xylanases are, intriguing in that catalysis is performed via a covalent intermediate, adopting an unusual (2,5)B (boat) conformation, a conformation which also, fulfils the stereochemical constraints of the oxocarbenium ion-like, transition state. Here, the 1.9 A structure of a nucleophile, E94A, mutant, of the Xyn11 from Bacillus agaradhaerens in complex with xylotriose is, presented. Intriguingly, this complex also adopts the (2,5)B conformation, in the -1 subsite, with the vacant space provided by the Glu-->Ala, mutation allowing the sugar to adopt the alpha-configuration at C1. The, structure of the covalent 2-deoxy-2-fluoroxylobiosyl-enzyme intermediate, has been extended to atomic (1.1 A) resolution.
About this Structure
1H4H is a Single protein structure of sequence from Bacillus agaradhaerens. 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
Oligosaccharide binding to family 11 xylanases: both covalent intermediate and mutant product complexes display (2,5)B conformations at the active centre., Sabini E, Wilson KS, Danielsen S, Schulein M, Davies GJ, Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1344-7. Epub 2001, Aug 23. PMID:11526340
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