6h07: Difference between revisions
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The | ==X-ray structure of Lactobacillus brevis alcohol dehydrogenase== | ||
<StructureSection load='6h07' size='340' side='right'caption='[[6h07]], [[Resolution|resolution]] 1.48Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6h07]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_casei_g"_von_freudenreich_and_thoni_1904 "bacillus casei g" von freudenreich and thoni 1904]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H07 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H07 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6h1m|6h1m]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">radh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1580 "Bacillus casei g" von Freudenreich and Thoni 1904])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6h07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h07 OCA], [http://pdbe.org/6h07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h07 RCSB], [http://www.ebi.ac.uk/pdbsum/6h07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h07 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:30511668</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6h07" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus casei g von freudenreich and thoni 1904]] | |||
[[Category: Large Structures]] | |||
[[Category: Biggel, P]] | |||
[[Category: Hekmat, D]] | |||
[[Category: Hermann, J]] | |||
[[Category: Nowotny, P]] | |||
[[Category: Schneider, S]] | |||
[[Category: Weuster-Botz, D]] | |||
[[Category: Magnesium dependence]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: R-specific alcohol dehydrogenase]] | |||
[[Category: Short chain reductases/dehydrogenase]] | |||
