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3A64

Crystal structure of CcCel6C, a glycoside hydrolase family 6 enzyme, from Coprinopsis cinerea

Summary for 3A64
Entry DOI10.2210/pdb3a64/pdb
DescriptorCellobiohydrolase, MAGNESIUM ION (3 entities in total)
Functional Keywordsseven-stranded beta-alpha barrel, cellulase, glycoside hydrolase family 6, cellobiohydrolase, hydrolase
Biological sourceCoprinopsis cinerea (Inky cap fungus)
Total number of polymer chains1
Total formula weight43655.41
Authors
Liu, Y.,Yoshida, M.,Kurakata, Y.,Miyazaki, T.,Nishikawa, A.,Tonozuka, T. (deposition date: 2009-08-21, release date: 2009-09-01, Last modification date: 2024-11-20)
Primary citationLiu, Y.,Yoshida, M.,Kurakata, Y.,Miyazaki, T.,Igarashi, K.,Samejima, M.,Fukuda, K.,Nishikawa, A.,Tonozuka, T.
Crystal structure of a glycoside hydrolase family 6 enzyme, CcCel6C, a cellulase constitutively produced by Coprinopsis cinerea
Febs J., 277:1532-1542, 2010
Cited by
PubMed Abstract: The basidiomycete Coprinopsis cinerea produces the glycoside hydrolase family 6 enzyme CcCel6C at low and constitutive levels. CcCel6C exhibits unusual cellobiohydrolase activity; it hydrolyses carboxymethyl cellulose, which is a poor substrate for typical cellobiohydrolases. Here, we determined the crystal structures of CcCel6C unbound and in complex with p-nitrophenyl beta-D-cellotrioside and cellobiose. CcCel6C consists of a distorted seven-stranded beta/alpha barrel and has an enclosed tunnel, which is observed in other cellobiohydrolases from ascomecetes Hypocrea jecorina (HjeCel6A) and Humicola insolens (HinCel6A). In HjeCel6A and HinCel6A, ligand binding produces a conformational change that narrows this tunnel. In contrast, the tunnel remains wide in CcCel6C and the conformational change appears to be less favourable than in HjeCel6A and HinCel6A. The ligand binding cleft for subsite -3 of CcCel6C is also wide and is rather similar to that of endoglucanase. These results suggest that the open tunnel and the wide cleft are suitable for the hydrolysis of carboxymethyl cellulose.
PubMed: 20148970
DOI: 10.1111/j.1742-4658.2010.07582.x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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