3u4a

Publication Abstract from PubMed

A recent metagenomic analysis sequenced a switchgrass-adapted compost community to identify enzymes from microorganisms that were specifically adapted to switchgrass under thermophilic conditions. These enzymes are being examined as part of the pretreatment process for the production of "second-generation" biofuels. Among the enzymes discovered was JMB19063, a novel three-domain beta-glucosidase that belongs to the GH3 (glycoside hydrolase 3) family. Here, we report the structure of JMB19063 in complex with glucose and the catalytic variant D261N crystallized in the presence of cellopentaose. JMB19063 is first structure of a dimeric member of the GH3 family, and we demonstrate that dimerization is required for catalytic activity. Arg-587 and Phe-598 from the C-terminal domain of the opposing monomer are shown to interact with bound ligands in the D261N structure. Enzyme assays confirmed that these residues are absolutely essential for full catalytic activity.

From soil to structure, a novel dimeric beta-glucosidase belonging to glycoside hydrolase family 3 isolated from compost using metagenomic analysis.,McAndrew RP, Park JI, Heins RA, Reindl W, Friedland GD, D'haeseleer P, Northen T, Sale KL, Simmons BA, Adams PD J Biol Chem. 2013 May 24;288(21):14985-92. doi: 10.1074/jbc.M113.458356. Epub , 2013 Apr 11. PMID:23580647^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.