4d1i
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The structure of the GH35 beta-galactosidase Bgl35A from Cellvibrio japonicus
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Structural highlights
FunctionPublication Abstract from PubMedThe degradation of plant biomass by saprophytes is an ecologically important part of the global carbon cycle, which has also inspired a vast diversity of industrial enzyme applications. The xyloglucans (XyGs) constitute a family of ubiquitous and abundant plant cell wall polysaccharides, yet the enzymology of XyG saccharification is poorly studied. Here, we present the identification and molecular characterization of a complex genetic locus that is required for xyloglucan utilization by the model saprophyte Cellvibrio japonicus. In harness, transcriptomics, reverse genetics, enzyme kinetics, and structural biology indicate that the encoded cohort of an alpha-xylosidase, a beta-galactosidase, and an alpha-l-fucosidase is specifically adapted for efficient, concerted saccharification of dicot (fucogalacto)xyloglucan oligosaccharides following import into the periplasm via an associated TonB-dependent receptor. The data support a biological model of xyloglucan degradation by C. japonicus with striking similarities - and notable differences - to the complex polysaccharide utilization loci of the Bacteroidetes. A complex gene locus enables xyloglucan utilization in the model saprophyte Cellvibrio japonicus.,Larsbrink J, Thompson AJ, Lundqvist M, Gardner JG, Davies GJ, Brumer H Mol Microbiol. 2014 Oct;94(2):418-33. doi: 10.1111/mmi.12776. Epub 2014 Sep 17. PMID:25171165[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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