1e0x
From Proteopedia
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|PDB= 1e0x |SIZE=350|CAPTION= <scene name='initialview01'>1e0x</scene>, resolution 1.65Å | |PDB= 1e0x |SIZE=350|CAPTION= <scene name='initialview01'>1e0x</scene>, resolution 1.65Å | ||
|SITE= <scene name='pdbsite=AC1:X2f+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Xys+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:X2f+Binding+Site+For+Chain+B'>AC3</scene>, <scene name='pdbsite=AC4:Xys+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=ACA:Catalytic+Acid/Base+Chain+A'>ACA</scene>, <scene name='pdbsite=ACB:Catalytic+Acid/Base+Chain+B'>ACB</scene>, <scene name='pdbsite=NUA:Catalytic+Nucleophile+Chain+A'>NUA</scene> and <scene name='pdbsite=NUB:Catalytic+Nucleophile+Chain+B'>NUB</scene> | |SITE= <scene name='pdbsite=AC1:X2f+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Xys+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:X2f+Binding+Site+For+Chain+B'>AC3</scene>, <scene name='pdbsite=AC4:Xys+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=ACA:Catalytic+Acid/Base+Chain+A'>ACA</scene>, <scene name='pdbsite=ACB:Catalytic+Acid/Base+Chain+B'>ACB</scene>, <scene name='pdbsite=NUA:Catalytic+Nucleophile+Chain+A'>NUA</scene> and <scene name='pdbsite=NUB:Catalytic+Nucleophile+Chain+B'>NUB</scene> | ||
| - | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=X2F:2-DEOXY-2-FLUORO+XYLOPYRANOSE'>X2F</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</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=1e0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0x OCA], [http://www.ebi.ac.uk/pdbsum/1e0x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e0x RCSB]</span> | ||
}} | }} | ||
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[[Category: Morosoli, R.]] | [[Category: Morosoli, R.]] | ||
[[Category: Shareck, F.]] | [[Category: Shareck, F.]] | ||
| - | [[Category: GOL]] | ||
[[Category: glycoside hydrolase family 10]] | [[Category: glycoside hydrolase family 10]] | ||
[[Category: glycosyl-enzyme intermediate]] | [[Category: glycosyl-enzyme 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 19:52:48 2008'' |
Revision as of 16:52, 30 March 2008
| |||||||
| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , and | ||||||
| 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 | ||||||
XYLANASE 10A FROM SREPTOMYCES LIVIDANS. XYLOBIOSYL-ENZYME INTERMEDIATE AT 1.65 A
Overview
Endoxylanases are a group of enzymes that hydrolyze the beta-1, 4-linked xylose backbone of xylans. They are predominantly found in two discrete sequence families known as glycoside hydrolase families 10 and 11. The Streptomyces lividans xylanase Xyl10A is a family 10 enzyme, the native structure of which has previously been determined by x-ray crystallography at a 2.6 A resolution (Derewenda, U., Swenson, L., Green, R., Wei, Y., Morosoli, R., Shareck, F., Kluepfel, D., and Derewenda, Z. S. (1994) J. Biol. Chem. 269, 20811-20814). Here, we report the native structure of Xyl10A refined at a resolution of 1.2 A, which reveals many features such as the rare occurrence of a discretely disordered disulfide bond between residues Cys-168 and Cys-201. In order to investigate substrate binding and specificity in glycoside hydrolase family 10, the covalent xylobiosyl enzyme and the covalent cellobiosyl enzyme intermediates of Xyl10A were trapped through the use of appropriate 2-fluoroglycosides. The alpha-linked intermediate with the nucleophile, Glu-236, is in a (4)C(1) chair conformation as previously observed in the family 10 enzyme Cex from Cellulomonas fimi (Notenboom, V., Birsan, C., Warren, R. A. J., Withers, S. G., and Rose, D. R. (1998) Biochemistry 37, 4751-4758). The different interactions of Xyl10A with the xylobiosyl and cellobiosyl moieties, notably conformational changes in the -2 and -1 subsites, together with the observed kinetics on a range of aryl glycosides, shed new light on substrate specificity in glycoside hydrolase family 10.
About this Structure
1E0X is a Single protein structure of sequence from Streptomyces lividans. Full crystallographic information is available from OCA.
Reference
Substrate specificity in glycoside hydrolase family 10. Structural and kinetic analysis of the Streptomyces lividans xylanase 10A., Ducros V, Charnock SJ, Derewenda U, Derewenda ZS, Dauter Z, Dupont C, Shareck F, Morosoli R, Kluepfel D, Davies GJ, J Biol Chem. 2000 Jul 28;275(30):23020-6. PMID:10930426
Page seeded by OCA on Sun Mar 30 19:52:48 2008
Categories: Endo-1,4-beta-xylanase | Single protein | Streptomyces lividans | Charnock, S J. | Dauter, Z. | Davies, G J. | Derewenda, U. | Derewenda, Z S. | Ducros, V. | Dupont, C. | Kluepfel, D. | Morosoli, R. | Shareck, F. | Glycoside hydrolase family 10 | Glycosyl-enzyme intermediate | Xylan degradation | Xylanase
