1g01

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[[Image:1g01.gif|left|200px]]
[[Image:1g01.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1g01 |SIZE=350|CAPTION= <scene name='initialview01'>1g01</scene>, resolution 1.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1g01", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1g01| PDB=1g01 | SCENE= }}
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|RELATEDENTRY=[[1g0c|1G0C]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g01 OCA], [http://www.ebi.ac.uk/pdbsum/1g01 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g01 RCSB]</span>
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}}
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'''ALKALINE CELLULASE K CATALYTIC DOMAIN'''
'''ALKALINE CELLULASE K CATALYTIC DOMAIN'''
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[[Category: Shirai, T.]]
[[Category: Shirai, T.]]
[[Category: Yamane, T.]]
[[Category: Yamane, T.]]
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[[Category: alpha/beta barrel]]
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[[Category: Alpha/beta barrel]]
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[[Category: tim barrel]]
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[[Category: Tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:57:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:33:40 2008''
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Revision as of 13:57, 2 May 2008

Image:1g01.gif

Template:STRUCTURE 1g01

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.. 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 Page seeded by OCA on Fri May 2 16:57:37 2008

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