4wva

Crystal structure of GH63 mannosylglycerate hydrolase from Thermus thermophilus HB8 in complex with Tris

spinqualitylabelsall models 4wva, resolution 1.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wva is a 2 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.67Å Ligands: CL, MPD, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5SJN0_THET8 Publication Abstract from PubMed Glycoside hydrolase family 63 (GH63) proteins are found in eukaryotes such as processing alpha-glucosidase I and also many bacteria and archaea. Recent studies have identified two bacterial and one plant GH63 mannosylglycerate hydrolases that act on both glucosylglycerate and mannosylglycerate, which are compatible solutes found in many thermophilic prokaryotes and some plants. Here we report the 1.67-A crystal structure of one of these GH63 mannosylglycerate hydrolases, Tt8MGH from Thermus thermophilus HB8, which is 99% homologous to mannosylglycerate hydrolase from T.thermophilus HB27. Tt8MGH consists of a single (alpha/alpha)6-barrel catalytic domain with two additional helices and two long loops which form a homotrimer. The structures of this protein in complexes with glucose or glycerate were also determined at 1.77- or 2.10-A resolution, respectively. A comparison of these structures revealed that the conformations of three flexible loops were largely different from each other. The conformational changes may be induced by ligand binding and serve to form finger-like structures for holding substrates. These findings represent the first-ever proposed substrate recognition mechanism for GH63 mannosylglycerate hydrolase. Crystal structure and substrate-binding mode of GH63 mannosylglycerate hydrolase from Thermus thermophilus HB8.,Miyazaki T, Ichikawa M, Iino H, Nishikawa A, Tonozuka T J Struct Biol. 2015 Feb 21. pii: S1047-8477(15)00037-4. doi:, 10.1016/j.jsb.2015.02.006. PMID:25712767 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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