This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1h4h
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[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 /> | ||
| Line 8: | Line 7: | ||
==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== | ||
| Line 27: | Line 26: | ||
[[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
|
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
Page seeded by OCA on Tue Dec 18 15:58:37 2007
