1nq6
From Proteopedia
(New page: 200px<br /><applet load="1nq6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nq6, resolution 1.78Å" /> '''Crystal Structure of...) |
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| - | [[Image:1nq6.jpg|left|200px]]<br /><applet load="1nq6" size=" | + | [[Image:1nq6.jpg|left|200px]]<br /><applet load="1nq6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nq6, resolution 1.78Å" /> | caption="1nq6, resolution 1.78Å" /> | ||
'''Crystal Structure of the catalytic domain of xylanase A from Streptomyces halstedii JM8'''<br /> | '''Crystal Structure of the catalytic domain of xylanase A from Streptomyces halstedii JM8'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Xylanases hydrolyze the beta-1,4-linked xylose backbone of xylans. They | + | 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 Structure== | ==About this Structure== | ||
| - | 1NQ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_halstedii Streptomyces halstedii] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http:// | + | 1NQ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_halstedii Streptomyces halstedii] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQ6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Canals, A.]] | [[Category: Canals, A.]] | ||
[[Category: Coll, M.]] | [[Category: Coll, M.]] | ||
| - | [[Category: Gomis-Ruth, F | + | [[Category: Gomis-Ruth, F X.]] |
| - | [[Category: Santamaria, R | + | [[Category: Santamaria, R I.]] |
| - | [[Category: Vega, M | + | [[Category: Vega, M C.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: glycoside hydrolase family 10]] | [[Category: glycoside hydrolase family 10]] | ||
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[[Category: xylanase]] | [[Category: xylanase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:49 2008'' |
Revision as of 12:09, 21 February 2008
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Crystal Structure of the catalytic domain of xylanase A from Streptomyces halstedii JM8
Overview
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 Structure
1NQ6 is a Single protein structure of sequence from Streptomyces halstedii with as ligand. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.
Reference
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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