6h1m | pdb_00006h1m

Neutron structure of Lactobacillus brevis alcohol dehydrogenase

spinqualitylabelsall models 6h1m, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6h1m is a 1 chain structure with sequence from Levilactobacillus brevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Neutron Diffraction, Resolution 2.15Å Ligands: MG, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q84EX5_LEVBR Publication Abstract from PubMed Lactobacillus brevis alcohol dehydrogenase (LbADH) is a well studied homotetrameric enzyme which catalyzes the enantioselective reduction of prochiral ketones to the corresponding secondary alcohols. LbADH is stable and enzymatically active at elevated temperatures and accepts a broad range of substrates, making it a valuable tool in industrial biocatalysis. Here, the expression, purification and crystallization of LbADH to generate large, single crystals with a volume of up to 1 mm(3) suitable for neutron diffraction studies are described. Neutron diffraction data were collected from an H/D-exchanged LbADH crystal using the BIODIFF instrument at the Heinz Maier-Leibnitz Zentrum (MLZ), Garching, Germany to a resolution dmin of 2.15 A in 16 days. This allowed the first neutron crystal structure of LbADH to be determined. The neutron structure revealed new details of the hydrogen-bonding network originating from the ion-binding site of LbADH and provided new insights into the reasons why divalent magnesium (Mg(2+)) or manganese (Mn(2+)) ions are necessary for its activity. X-ray diffraction data were obtained from the same crystal at the European Synchrotron Radiation Facility (ESRF), Grenoble, France to a resolution dmin of 1.48 A. The high-resolution X-ray structure suggested partial occupancy of Mn(2+) and Mg(2+) at the ion-binding site. This is supported by the different binding affinity of Mn(2+) and Mg(2+) to the tetrameric structure calculated via free-energy molecular-dynamics simulations. Neutron and X-ray crystal structures of Lactobacillus brevis alcohol dehydrogenase reveal new insights into hydrogen-bonding pathways.,Hermann J, Nowotny P, Schrader TE, Biggel P, Hekmat D, Weuster-Botz D Acta Crystallogr F Struct Biol Commun. 2018 Dec 1;74(Pt 12):754-764. doi:, 10.1107/S2053230X18015273. Epub 2018 Nov 26. PMID:30511668 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alcohol dehydrogenase 3D structures

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