| http://purl.uniprot.org/citations/30511668 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/30511668 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/30511668 | http://www.w3.org/2000/01/rdf-schema#comment | "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 mm3 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 Å 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 (Mg2+) or manganese (Mn2+) 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 Å. The high-resolution X-ray structure suggested partial occupancy of Mn2+ and Mg2+ at the ion-binding site. This is supported by the different binding affinity of Mn2+ and Mg2+ to the tetrameric structure calculated via free-energy molecular-dynamics simulations."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.org/dc/terms/identifier | "doi:10.1107/S2053230X18015273"xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.org/dc/terms/identifier | "doi:10.1107/s2053230x18015273"xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/author | "Weuster-Botz D."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/author | "Weuster-Botz D."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/author | "Hermann J."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/author | "Hermann J."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/author | "Nowotny P."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/author | "Nowotny P."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/author | "Schrader T.E."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/author | "Schrader T.E."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/author | "Biggel P."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/author | "Biggel P."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/author | "Hekmat D."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/author | "Hekmat D."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/name | "Acta Crystallogr. F Struct. Biol. Commun."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/name | "Acta Crystallogr F Struct Biol Commun"xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/pages | "754-764"xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/pages | "754-764"xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/title | "Neutron and X-ray crystal structures of Lactobacillus brevis alcohol dehydrogenase reveal new insights into hydrogen-bonding pathways."xsd:string |
| http://purl.uniprot.org/citations/30511668 | http://purl.uniprot.org/core/title | "Neutron and X-ray crystal structures of Lactobacillus brevis alcohol dehydrogenase reveal new insights into hydrogen-bonding pathways."xsd:string |