6csj
From Proteopedia
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(New page: '''Unreleased structure''' The entry 6csj is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of a Bacillus coagulans polyol dehydrogenase double mutant with an acquired D-lactate dehydrogenase activity== | |
| + | <StructureSection load='6csj' size='340' side='right'caption='[[6csj]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6csj]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Weizmannia_coagulans Weizmannia coagulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CSJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.395Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6csj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6csj OCA], [https://pdbe.org/6csj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6csj RCSB], [https://www.ebi.ac.uk/pdbsum/6csj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6csj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A150JSL8_WEICA A0A150JSL8_WEICA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | During adaptive metabolic evolution a native glycerol dehydrogenase (GDH) acquired a d-lactate dehydrogenase (LDH) activity. Two active-site amino acid changes were detected in the altered protein. Biochemical studies along with comparative structure analysis using an X-ray crystallographic structure model of the protein with the two different amino acids allowed prediction of pyruvate binding into the active site. We propose that the F245S alteration increased the capacity of the glycerol binding site and facilitated hydrogen bonding between the S245 gamma-O and the C1 carboxylate of pyruvate. To our knowledge, this is the first GDH to gain LDH activity due to an active site amino acid change, a desired result of in vivo enzyme evolution. | ||
| - | + | Kinetic characterization and structure analysis of an altered polyol dehydrogenase with d-lactate dehydrogenase activity.,Chauliac D, Wang Q, St John FJ, Jones G, Hurlbert JC, Ingram LO, Shanmugam KT Protein Sci. 2020 Dec;29(12):2387-2397. doi: 10.1002/pro.3963. Epub 2020 Oct 24. PMID:33020946<ref>PMID:33020946</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6csj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Weizmannia coagulans]] | ||
| + | [[Category: Hurlbert JC]] | ||
| + | [[Category: StJohn FJ]] | ||
Current revision
Structure of a Bacillus coagulans polyol dehydrogenase double mutant with an acquired D-lactate dehydrogenase activity
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