Structural highlights
Publication Abstract from PubMed
The crystal structure of the N-terminal putative catalytic domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea (CcGH131A) was determined. The structure of CcGH131A was found to be composed of a beta-jelly roll fold and mainly consisted of two beta-sheets, sheet-A and sheet-B. A concave of sheet-B, the possible active site, was wide and shallow, and three glycerol molecules were present in the concave. Arg96, Glu98, Glu138, and His218 are likely to be catalytically critical residues, and it was suggested that the catalytic mechanism of CcGH131A is different from that of typical glycosidases.
Crystal structure of the N-terminal domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea.,Miyazaki T, Yoshida M, Tamura M, Tanaka Y, Umezawa K, Nishikawa A, Tonozuka T FEBS Lett. 2013 Jul 11;587(14):2193-8. doi: 10.1016/j.febslet.2013.05.041. Epub, 2013 May 24. PMID:23711369[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Miyazaki T, Yoshida M, Tamura M, Tanaka Y, Umezawa K, Nishikawa A, Tonozuka T. Crystal structure of the N-terminal domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea. FEBS Lett. 2013 Jul 11;587(14):2193-8. doi: 10.1016/j.febslet.2013.05.041. Epub, 2013 May 24. PMID:23711369 doi:10.1016/j.febslet.2013.05.041
