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1hix

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[[Image:1hix.gif|left|200px]]<br /><applet load="1hix" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hix.gif|left|200px]]
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caption="1hix, resolution 2.0&Aring;" />
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'''CRYSTALLOGRAPHIC ANALYSES OF FAMILY 11 ENDO-BETA-1,4-XYLANASE XYL1 FROM STREPTOMYCES SP. S38'''<br />
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{{Structure
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|PDB= 1hix |SIZE=350|CAPTION= <scene name='initialview01'>1hix</scene>, resolution 2.0&Aring;
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|SITE=
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|LIGAND=
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|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]
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|GENE= XYL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35621 Streptomyces mobaraensis])
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}}
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'''CRYSTALLOGRAPHIC ANALYSES OF FAMILY 11 ENDO-BETA-1,4-XYLANASE XYL1 FROM STREPTOMYCES SP. S38'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1HIX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_mobaraensis Streptomyces mobaraensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HIX OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11717493 11717493]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11717493 11717493]
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: xylan degradation]]
[[Category: xylan degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:37:36 2008''

Revision as of 09:37, 20 March 2008


PDB ID 1hix

Drag the structure with the mouse to rotate
, resolution 2.0Å
Gene: XYL1 (Streptomyces mobaraensis)
Activity: Endo-1,4-beta-xylanase, with EC number 3.2.1.8
Coordinates: save as pdb, mmCIF, xml



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. 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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