6m5n
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Apo-Form Structure of Borneol Dehydrogenase== | |
| + | <StructureSection load='6m5n' size='340' side='right'caption='[[6m5n]], [[Resolution|resolution]] 1.84Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6m5n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._TCU-HL1 Pseudomonas sp. TCU-HL1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M5N 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]] 1.84Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6m5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m5n OCA], [https://pdbe.org/6m5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m5n RCSB], [https://www.ebi.ac.uk/pdbsum/6m5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m5n ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A1B3EB36_9PSED A0A1B3EB36_9PSED] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | During the microbial degradation of borneol, a bicyclic plant monoterpene, it is first converted into camphor by borneol dehydrogenase (BDH) and then enters a known camphor-degradation pathway. Previously, a recombinant Pseudomonas BDH was found in inclusion bodies when expressed in Escherichia coli. After refolding, it was still unstable and was difficult to concentrate. Here, the protein-expression conditions were improved by changing the medium from lysogeny broth to Terrific Broth, yielding a soluble form of the enzyme with higher activity. The protein was crystallized and its 3D structure was determined by X-ray diffraction. Like other known homologues such as quinuclidinone reductase, the protein forms a tetramer with subunits containing Rossmann folds. Structural comparison revealed major differences in the C-terminal helices and the associated loops. It is likely that these regions contain the determinants for substrate recognition. | ||
| - | + | Structural characterization of borneol dehydrogenase from Pseudomonas sp. TCU-HL1.,Khine AA, Chen HP, Huang KF, Ko TP Acta Crystallogr F Struct Biol Commun. 2020 Jul 1;76(Pt 7):309-313. doi: , 10.1107/S2053230X20008584. Epub 2020 Jul 1. PMID:32627746<ref>PMID:32627746</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6m5n" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas sp. TCU-HL1]] | ||
| + | [[Category: Chen HP]] | ||
| + | [[Category: Huang KF]] | ||
| + | [[Category: Khine AA]] | ||
| + | [[Category: Ko TP]] | ||
Current revision
Apo-Form Structure of Borneol Dehydrogenase
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