1hix: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1hix" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hix, resolution 2.0Å" /> '''CRYSTALLOGRAPHIC ANAL...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1hix.gif|left|200px]]<br /><applet load="1hix" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1hix.gif|left|200px]]<br /><applet load="1hix" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1hix, resolution 2.0&Aring;" />
caption="1hix, resolution 2.0&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HIX OCA].  
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==
Line 17: Line 17:
[[Category: Depiereux, E.]]
[[Category: Depiereux, E.]]
[[Category: Dusart, J.]]
[[Category: Dusart, J.]]
[[Category: Frere, J.M.]]
[[Category: Frere, J M.]]
[[Category: Georis, J.]]
[[Category: Georis, J.]]
[[Category: Wouters, J.]]
[[Category: Wouters, J.]]
Line 23: Line 23:
[[Category: xylan degradation]]
[[Category: xylan degradation]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:39:54 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:44 2008''