1nq6: Difference between revisions
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|PDB= 1nq6 |SIZE=350|CAPTION= <scene name='initialview01'>1nq6</scene>, resolution 1.78Å | |PDB= 1nq6 |SIZE=350|CAPTION= <scene name='initialview01'>1nq6</scene>, resolution 1.78Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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= xysA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1944 Streptomyces halstedii]) | |GENE= xysA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1944 Streptomyces halstedii]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nq6 OCA], [http://www.ebi.ac.uk/pdbsum/1nq6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nq6 RCSB]</span> | |||
}} | }} | ||
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[[Category: Santamaria, R I.]] | [[Category: Santamaria, R I.]] | ||
[[Category: Vega, M C.]] | [[Category: Vega, M C.]] | ||
[[Category: glycoside hydrolase family 10]] | [[Category: glycoside hydrolase family 10]] | ||
[[Category: xylan degradation]] | [[Category: xylan degradation,]] | ||
[[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 22:33:57 2008'' | ||
Revision as of 22:33, 30 March 2008
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| , resolution 1.78Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | xysA (Streptomyces halstedii) | ||||||
| Activity: | Endo-1,4-beta-xylanase, with EC number 3.2.1.8 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the catalytic domain of xylanase A from Streptomyces halstedii JM8
OverviewOverview
Xylanases hydrolyze the beta-1,4-linked xylose backbone of xylans. They are of increasing interest in the paper and food industries for their pre-bleaching and bio-pulping applications. Such industries demand new xylanases to cover a wider range of cleavage specificity, activity and stability. The catalytic domain of xylanase Xys1 from Streptomyces halstedii JM8 was expressed, purified and crystallized and native data were collected to 1.78 A resolution with an R(merge) of 4.4%. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.05, b = 79.60, c = 87.80 A. The structure was solved by the molecular-replacement method using the structure of the homologue Xyl10A from Streptomyces lividans. In a similar manner to other members of its family, Xys1 folds to form a standard (beta/alpha)(8) barrel with the two catalytic functions, the acid/base and the nucleophile, at its C-terminal side. The overall structure is described and compared with those of related xylanases.
About this StructureAbout this Structure
1NQ6 is a Single protein structure of sequence from Streptomyces halstedii. Full crystallographic information is available from OCA.
ReferenceReference
Structure of xylanase Xys1delta from Streptomyces halstedii., Canals A, Vega MC, Gomis-Ruth FX, Diaz M, Santamaria R RI, Coll M, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1447-53. Epub 2003, Jul 23. PMID:12876348
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