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From Proteopedia
Structure of Fungal beta-mannosidase (GH2) from Trichoderma harzianum
Structural highlights
FunctionPublication Abstract from PubMedHemicellulose is an important part of the plant cell wall biomass relevant to cellulosic ethanol technologies. beta-Mannosidases are enzymes capable of cleavage of non-reducing residues of beta-D-mannose from beta-D-mannosides and hemicellulose mannose-containing polysaccharides, such as mannans and galactomannans. beta-Mannosidases are distributed between glycoside hydrolase (GH) families 1, 2 and 5 with only a handful of the enzymes being structurally characterized to date. The only published X-ray structure of GH2 mannosidase is that of bacterial Bacteroides thetaiotaomicron enzyme. No structures of eukaryotic mannosidases of this family are currently available. To fill this gap we set out to solve the structure of Trichoderma harzianum GH2 beta-mannosidase and to refine it to 1.9 A resolution. Structural comparisons of the T. harzianum GH2 beta-mannosidase highlight similarities in its structural architecture with other members of GH2 family, reveal molecular mechanism of the beta-mannosides binding and recognition and shed light on its putative galactomannan binding site. This article is protected by copyright. All rights reserved. Insights Into Structure and Function of Fungal beta-mannosidases from Glycoside Hydrolase Family 2 Based on Multiple Crystal Structures of T. harzianum Enzyme.,Nascimento AS, Muniz JR, Aparicio R, Golubev AM, Polikarpov I FEBS J. 2014 Jun 26. doi: 10.1111/febs.12894. PMID:24975648[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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