1g01

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(New page: 200px<br /><applet load="1g01" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g01, resolution 1.9&Aring;" /> '''ALKALINE CELLULASE K ...)
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[[Image:1g01.gif|left|200px]]<br /><applet load="1g01" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1g01, resolution 1.9&Aring;" />
caption="1g01, resolution 1.9&Aring;" />
'''ALKALINE CELLULASE K CATALYTIC DOMAIN'''<br />
'''ALKALINE CELLULASE K CATALYTIC DOMAIN'''<br />
==Overview==
==Overview==
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The crystal structure of the catalytic domain of alkaline cellulase K was, determined at 1.9 A resolution. Because of the most alkaliphilic nature, and it's highest activity at pH 9.5, it is used commercially in laundry, detergents. An analysis of the structural bases of the alkaliphilic, character of the enzyme suggested a mechanism similar to that previously, proposed for alkaline proteases, that is, an increase in the number of, Arg, His, and Gln residues, and a decrease in Asp and Lys residues. Some, ion pairs were formed by the gained Arg residues, which is similar to what, has been found in the alkaline proteases. Lys-Asp ion pairs are disfavored, and partly replaced with Arg-Asp ion pairs. The alkaline adaptation, appeared to be a remodeling of ion pairs so that the charge balance is, kept in the high pH range.
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The crystal structure of the catalytic domain of alkaline cellulase K was determined at 1.9 A resolution. Because of the most alkaliphilic nature and it's highest activity at pH 9.5, it is used commercially in laundry detergents. An analysis of the structural bases of the alkaliphilic character of the enzyme suggested a mechanism similar to that previously proposed for alkaline proteases, that is, an increase in the number of Arg, His, and Gln residues, and a decrease in Asp and Lys residues. Some ion pairs were formed by the gained Arg residues, which is similar to what has been found in the alkaline proteases. Lys-Asp ion pairs are disfavored and partly replaced with Arg-Asp ion pairs. The alkaline adaptation appeared to be a remodeling of ion pairs so that the charge balance is kept in the high pH range.
==About this Structure==
==About this Structure==
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1G01 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with CD and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1G01 OCA].
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1G01 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1G01 OCA].
==Reference==
==Reference==
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[[Category: tim barrel]]
[[Category: tim barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:34:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:31 2008''

Revision as of 10:44, 21 February 2008

Image:1g01.gif

1g01, resolution 1.9Å

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ALKALINE CELLULASE K CATALYTIC DOMAIN

Overview

The crystal structure of the catalytic domain of alkaline cellulase K was determined at 1.9 A resolution. Because of the most alkaliphilic nature and it's highest activity at pH 9.5, it is used commercially in laundry detergents. An analysis of the structural bases of the alkaliphilic character of the enzyme suggested a mechanism similar to that previously proposed for alkaline proteases, that is, an increase in the number of Arg, His, and Gln residues, and a decrease in Asp and Lys residues. Some ion pairs were formed by the gained Arg residues, which is similar to what has been found in the alkaline proteases. Lys-Asp ion pairs are disfavored and partly replaced with Arg-Asp ion pairs. The alkaline adaptation appeared to be a remodeling of ion pairs so that the charge balance is kept in the high pH range.

About this Structure

1G01 is a Single protein structure of sequence from Bacillus sp. with and as ligands. Active as Cellulase, with EC number 3.2.1.4 Full crystallographic information is available from OCA.

Reference

Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme., Shirai T, Ishida H, Noda J, Yamane T, Ozaki K, Hakamada Y, Ito S, J Mol Biol. 2001 Jul 27;310(5):1079-87. PMID:11501997

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