4d1j

The structure of the GH35 beta-galactosidase Bgl35A from Cellvibrio japonicas in complex with 1-Deoxygalactonojirimycin

spinqualitylabelsall models 4d1j, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d1j is a 8 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, DGJ, NA Related: 4d1i Activity: Beta-galactosidase, with EC number 3.2.1.23 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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