1xyz
From Proteopedia
(New page: 200px<br /><applet load="1xyz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xyz, resolution 1.4Å" /> '''A COMMON PROTEIN FOLD...) |
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| - | [[Image:1xyz.gif|left|200px]]<br /><applet load="1xyz" size=" | + | [[Image:1xyz.gif|left|200px]]<br /><applet load="1xyz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xyz, resolution 1.4Å" /> | caption="1xyz, resolution 1.4Å" /> | ||
'''A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES'''<br /> | '''A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of Clostridium thermocellum endoglucanase CelC, a member of | + | The structure of Clostridium thermocellum endoglucanase CelC, a member of the largest cellulase family (family A), has been determined at 2.15 A resolution. The protein folds into an (alpha/beta)8 barrel, with a deep active-site cleft generated by the insertion of a helical subdomain. The structure of the catalytic core of xylanase XynZ, which belongs to xylanase family F, has been determined at 1.4 A resolution. In spite of significant differences in substrate specificity and structure (including the absence of the helical subdomain), the general polypeptide folding pattern, architecture of the active site and catalytic mechanism of XynZ and CelC are similar, suggesting a common evolutionary origin. |
==About this Structure== | ==About this Structure== | ||
| - | 1XYZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. 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:// | + | 1XYZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. 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=1XYZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Endo-1,4-beta-xylanase]] | [[Category: Endo-1,4-beta-xylanase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Alzari, P | + | [[Category: Alzari, P M.]] |
[[Category: Dominguez, R.]] | [[Category: Dominguez, R.]] | ||
[[Category: Spinelli, S.]] | [[Category: Spinelli, S.]] | ||
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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 16:00:10 2008'' |
Revision as of 14:00, 21 February 2008
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A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES
Overview
The structure of Clostridium thermocellum endoglucanase CelC, a member of the largest cellulase family (family A), has been determined at 2.15 A resolution. The protein folds into an (alpha/beta)8 barrel, with a deep active-site cleft generated by the insertion of a helical subdomain. The structure of the catalytic core of xylanase XynZ, which belongs to xylanase family F, has been determined at 1.4 A resolution. In spite of significant differences in substrate specificity and structure (including the absence of the helical subdomain), the general polypeptide folding pattern, architecture of the active site and catalytic mechanism of XynZ and CelC are similar, suggesting a common evolutionary origin.
About this Structure
1XYZ is a Single protein structure of sequence from Clostridium thermocellum. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.
Reference
A common protein fold and similar active site in two distinct families of beta-glycanases., Dominguez R, Souchon H, Spinelli S, Dauter Z, Wilson KS, Chauvaux S, Beguin P, Alzari PM, Nat Struct Biol. 1995 Jul;2(7):569-76. PMID:7664125
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