6mgj

Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme

spinqualitylabelsall models 6mgj, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6mgj is a 8 chain structure with sequence from Paenibacillus odorifer. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: CL, GOL, MG, MSE, PE3, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1R0YRH0_9BACL Publication Abstract from PubMed Paenibacillus odorifer produces a single multimodular enzyme containing a glycoside hydrolase (GH) family 74 module (AIQ73809). Recombinant production and characterization of the GH74 module (PoGH74cat) revealed a highly specific, processive endo-xyloglucanase that can hydrolyze the polysaccharide backbone at both branched and unbranched positions. X-ray crystal structures obtained for the free enzyme and oligosaccharide complexes evidenced an extensive hydrophobic binding platform - the first in GH74 extending from subsites -4 to +6 - and unique mobile active-site loops. Site-directed mutagenesis revealed that glycine-476 was uniquely responsible for the promiscuous backbone-cleaving activity of PoGH74cat; replacement with tyrosine, which is conserved in many GH74 members, resulted in exclusive hydrolysis at unbranched glucose units. Likewise, systematic replacement of the hydrophobic platform residues constituting the positive subsites indicated their relative contributions to the processive mode of action. Specifically, W347 (+3 subsite) and W348 (+5 subsite) are essential for processivity, while W406 (+2 subsite) and Y372 (+6 subsite) are not strictly essential, but aid processivity. Structural enzymology reveals the molecular basis of substrate regiospecificity and processivity of an exemplar bacterial glycoside hydrolase family 74 endo-xyloglucanase.,Arnal G, Stogios PJ, Asohan J, Skarina T, Savchenko A, Brumer H Biochem J. 2018 Dec 19;475(24):3963-3978. doi: 10.1042/BCJ20180763. PMID:30463871 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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