1h4g
From Proteopedia
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|PDB= 1h4g |SIZE=350|CAPTION= <scene name='initialview01'>1h4g</scene>, resolution 1.10Å | |PDB= 1h4g |SIZE=350|CAPTION= <scene name='initialview01'>1h4g</scene>, resolution 1.10Å | ||
|SITE= <scene name='pdbsite=FXA:Fxp+Binding+Site+For+Chain+B'>FXA</scene> | |SITE= <scene name='pdbsite=FXA:Fxp+Binding+Site+For+Chain+B'>FXA</scene> | ||
| - | |LIGAND= <scene name='pdbligand=FXP:1,2,-DEOXY-2-FLUORO-4-O-BETA-D-XYLOPYRANOSYL-BETA-D-XYLOPYRANOSE'>FXP</scene> | + | |LIGAND= <scene name='pdbligand=FXP:1,2,-DEOXY-2-FLUORO-4-O-BETA-D-XYLOPYRANOSYL-BETA-D-XYLOPYRANOSE'>FXP</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4g OCA], [http://www.ebi.ac.uk/pdbsum/1h4g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h4g RCSB]</span> | ||
}} | }} | ||
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[[Category: Schulein, M.]] | [[Category: Schulein, M.]] | ||
[[Category: Wilson, K S.]] | [[Category: Wilson, K S.]] | ||
| - | [[Category: FXP]] | ||
| - | [[Category: SO4]] | ||
[[Category: boat conformation]] | [[Category: boat conformation]] | ||
[[Category: intermediate]] | [[Category: intermediate]] | ||
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[[Category: xylanase]] | [[Category: xylanase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:57:30 2008'' |
Revision as of 17:57, 30 March 2008
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| , resolution 1.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Endo-1,4-beta-xylanase, with EC number 3.2.1.8 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1H4G is a Single protein structure of sequence from Bacillus agaradhaerens. 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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