1G0C

ALKALINE CELLULASE K CATALYTIC DOMAIN-CELLOBIOSE COMPLEX

Summary for 1G0C

• Entry DOI: 10.2210/pdb1g0c/pdb
• Related: 1G01
• Related PRD ID: PRD_900005
• Descriptor: ENDOGLUCANASE, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, CADMIUM ION, ... (5 entities in total)
• Functional Keywords: alpha/beta barrel, tim-barrel, cellobiose complex, hydrolase
• Biological source: Bacillus sp.
• Total number of polymer chains: 1
• Total formula weight: 42073.87

Authors

Shirai, T.,Ishida, H.,Noda, J.,Yamane, T.,Ozaki, K.,Hakamada, Y.,Ito, S. (deposition date: 2000-10-05, release date: 2001-08-01, Last modification date: 2024-03-13)

Primary citation

Shirai, T.,Ishida, H.,Noda, J.,Yamane, T.,Ozaki, K.,Hakamada, Y.,Ito, S.
Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme.
J.Mol.Biol., 310:1079-1087, 2001

PubMed Abstract: 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.

PubMed: 11501997
DOI: 10.1006/jmbi.2001.4835

Experimental method

X-RAY DIFFRACTION (1.9 Å)