1hix
From Proteopedia
(New page: 200px<br /><applet load="1hix" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hix, resolution 2.0Å" /> '''CRYSTALLOGRAPHIC ANAL...) |
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| - | [[Image:1hix.gif|left|200px]]<br /><applet load="1hix" size=" | + | [[Image:1hix.gif|left|200px]]<br /><applet load="1hix" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hix, resolution 2.0Å" /> | caption="1hix, resolution 2.0Å" /> | ||
'''CRYSTALLOGRAPHIC ANALYSES OF FAMILY 11 ENDO-BETA-1,4-XYLANASE XYL1 FROM STREPTOMYCES SP. S38'''<br /> | '''CRYSTALLOGRAPHIC ANALYSES OF FAMILY 11 ENDO-BETA-1,4-XYLANASE XYL1 FROM STREPTOMYCES SP. S38'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Family 11 endo-beta-1,4-xylanases degrade xylan, the main constituent of | + | Family 11 endo-beta-1,4-xylanases degrade xylan, the main constituent of plant hemicelluloses, and have many potential uses in biotechnology. The structure of Xyl1, a family 11 endo-xylanase from Streptomyces sp. S38, has been solved. The protein crystallized from ammonium sulfate in the trigonal space group P321, with unit-cell parameters a = b = 71.49, c = 130.30 A, gamma = 120.0 degrees. The structure was solved at 2.0 A by X-ray crystallography using the molecular-replacement method and refined to a final R factor of 18.5% (R(free) = 26.9%). Xyl1 has the overall fold characteristic of family 11 xylanases, with two highly twisted beta-sheets defining a long cleft containing the two catalytic residues Glu87 and Glu177. |
==About this Structure== | ==About this Structure== | ||
| - | 1HIX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_mobaraensis Streptomyces mobaraensis]. 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:// | + | 1HIX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_mobaraensis Streptomyces mobaraensis]. 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=1HIX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Depiereux, E.]] | [[Category: Depiereux, E.]] | ||
[[Category: Dusart, J.]] | [[Category: Dusart, J.]] | ||
| - | [[Category: Frere, J | + | [[Category: Frere, J M.]] |
[[Category: Georis, J.]] | [[Category: Georis, J.]] | ||
[[Category: Wouters, J.]] | [[Category: Wouters, J.]] | ||
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[[Category: xylan degradation]] | [[Category: xylan degradation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:44 2008'' |
Revision as of 11:01, 21 February 2008
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CRYSTALLOGRAPHIC ANALYSES OF FAMILY 11 ENDO-BETA-1,4-XYLANASE XYL1 FROM STREPTOMYCES SP. S38
Overview
Family 11 endo-beta-1,4-xylanases degrade xylan, the main constituent of plant hemicelluloses, and have many potential uses in biotechnology. The structure of Xyl1, a family 11 endo-xylanase from Streptomyces sp. S38, has been solved. The protein crystallized from ammonium sulfate in the trigonal space group P321, with unit-cell parameters a = b = 71.49, c = 130.30 A, gamma = 120.0 degrees. The structure was solved at 2.0 A by X-ray crystallography using the molecular-replacement method and refined to a final R factor of 18.5% (R(free) = 26.9%). Xyl1 has the overall fold characteristic of family 11 xylanases, with two highly twisted beta-sheets defining a long cleft containing the two catalytic residues Glu87 and Glu177.
About this Structure
1HIX is a Single protein structure of sequence from Streptomyces mobaraensis. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.
Reference
Crystallographic analysis of family 11 endo-beta-1,4-xylanase Xyl1 from Streptomyces sp. S38., Wouters J, Georis J, Engher D, Vandenhaute J, Dusart J, Frere JM, Depiereux E, Charlier P, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1813-9. Epub 2001, Nov 21. PMID:11717493
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