1g01
From Proteopedia
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| , resolution 1.9Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Related: | 1G0C
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 20:33:40 2008
Categories: Bacillus sp. | Cellulase | Single protein | Hakamada, Y. | Ishida, H. | Ito, S. | Noda, J. | Ozaki, K. | Shirai, T. | Yamane, T. | Alpha/beta barrel | Tim barrel
