1cec
From Proteopedia
(New page: 200px<br /><applet load="1cec" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cec, resolution 2.15Å" /> '''A COMMON PROTEIN FOL...) |
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| - | [[Image:1cec.gif|left|200px]]<br /><applet load="1cec" size=" | + | [[Image:1cec.gif|left|200px]]<br /><applet load="1cec" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cec, resolution 2.15Å" /> | caption="1cec, resolution 2.15Å" /> | ||
'''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== | ||
| - | 1CEC 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/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Full crystallographic information is available from [http:// | + | 1CEC 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/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Clostridium thermocellum]] | [[Category: Clostridium thermocellum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Alzari, P | + | [[Category: Alzari, P M.]] |
[[Category: Dominguez, R.]] | [[Category: Dominguez, R.]] | ||
[[Category: cellulase]] | [[Category: cellulase]] | ||
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[[Category: glycosyl hydrolase]] | [[Category: glycosyl hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:11 2008'' |
Revision as of 10:05, 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
1CEC is a Single protein structure of sequence from Clostridium thermocellum. Active as Cellulase, with EC number 3.2.1.4 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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