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New page: left|200px<br /><applet load="1kwf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kwf, resolution 0.94Å" /> '''Atomic Resolution St...
 
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[[Image:1kwf.jpg|left|200px]]<br /><applet load="1kwf" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1kwf.jpg|left|200px]]<br /><applet load="1kwf" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1kwf, resolution 0.94&Aring;" />
caption="1kwf, resolution 0.94&Aring;" />
'''Atomic Resolution Structure of an Inverting Glycosidase in Complex with Substrate'''<br />
'''Atomic Resolution Structure of an Inverting Glycosidase in Complex with Substrate'''<br />


==Overview==
==Overview==
The crystal structure of Clostridium thermocellum endoglucanase CelA in, complex with cellopentaose has been determined at 0.94 A resolution. The, oligosaccharide occupies six D-glucosyl-binding subsites, three on either, side of the scissile glycosidic linkage. The substrate and product of the, reaction occupy different positions at the reducing end of the cleft, where an extended array of hydrogen-bonding interactions with water, molecules fosters the departure of the leaving group. Severe torsional, strain upon the bound substrate forces a distorted boat(2,5) B, conformation for the glucosyl residue bound at subsite -1, which, facilitates the formation of an oxocarbenium ion intermediate and might, favor the breakage of the sugar ring concomitant with catalysis.
The crystal structure of Clostridium thermocellum endoglucanase CelA in complex with cellopentaose has been determined at 0.94 A resolution. The oligosaccharide occupies six D-glucosyl-binding subsites, three on either side of the scissile glycosidic linkage. The substrate and product of the reaction occupy different positions at the reducing end of the cleft, where an extended array of hydrogen-bonding interactions with water molecules fosters the departure of the leaving group. Severe torsional strain upon the bound substrate forces a distorted boat(2,5) B conformation for the glucosyl residue bound at subsite -1, which facilitates the formation of an oxocarbenium ion intermediate and might favor the breakage of the sugar ring concomitant with catalysis.


==About this Structure==
==About this Structure==
1KWF 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KWF OCA].  
1KWF 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=1KWF OCA].  


==Reference==
==Reference==
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[[Category: Clostridium thermocellum]]
[[Category: Clostridium thermocellum]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Alzari, P.M.]]
[[Category: Alzari, P M.]]
[[Category: Beguin, P.]]
[[Category: Beguin, P.]]
[[Category: Costabel, M.]]
[[Category: Costabel, M.]]
[[Category: Guerin, D.M.A.]]
[[Category: Guerin, D M.A.]]
[[Category: Lamzin, V.]]
[[Category: Lamzin, V.]]
[[Category: Lascombe, M.B.]]
[[Category: Lascombe, M B.]]
[[Category: Souchon, H.]]
[[Category: Souchon, H.]]
[[Category: atomic resolution]]
[[Category: atomic resolution]]
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[[Category: reaction mechanism]]
[[Category: reaction mechanism]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:39 2008''