6jgk | pdb_00006jgk

Crystal structure of barley exohydrolaseI W434F mutant in complex with 4I,4III,4V-S-trithiocellohexaose

spinqualitylabelsall models 6jgk, resolution 1.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jgk is a 1 chain structure with sequence from Hordeum vulgare subsp. vulgare. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.66Å Ligands: 1PE, ACT, BGC, GOL, GS1, NAG, PRD_900034, SGC, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9XEI3_HORVV Publication Abstract from PubMed In the barley beta-D-glucan glucohydrolase, a glycoside hydrolase family 3 (GH3) enzyme, the Trp286/Trp434 clamp ensures beta-D-glucosides binding, which is fundamental for substrate hydrolysis during plant growth and development. We employ mutagenesis, high-resolution X-ray crystallography, and multi-scale molecular modelling methods to examine the binding and conformational behaviour of isomeric beta-D-glucosides during substrate-product assisted processive catalysis that operates in GH3 hydrolases. Enzyme kinetics reveals that the W434H mutant retains broad specificity, while W434A behaves as a strict (1,3)-beta-D-glucosidase. Investigations of reactant movements on the nanoscale reveal that processivity is sensitive to mutation-specific alterations of the tryptophan clamp. While wild-type and W434H utilise a lateral cavity for glucose displacement and sliding of (1,3)-linked hydrolytic products through the catalytic site without dissociation, consistent with their high hydrolytic rates, W434A does not adopt processive catalysis. Phylogenomic analyses of GH3 hydrolases disclose the evolutionary advantage of the tryptophan clamp that confers broad specificity, high catalytic efficiency, and processivity. The evolutionary advantage of an aromatic clamp in plant family 3 glycoside exo-hydrolases.,Luang S, Fernandez-Luengo X, Nin-Hill A, Streltsov VA, Schwerdt JG, Alonso-Gil S, Ketudat Cairns JR, Pradeau S, Fort S, Marechal JD, Masgrau L, Rovira C, Hrmova M Nat Commun. 2022 Sep 23;13(1):5577. doi: 10.1038/s41467-022-33180-5. PMID:36151080 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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