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4pze

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==Crystal structure of (S)-3-hydroxybutyryl-CoA dehydrogenase PaaH1 in complex with acetoacetyl-CoA==
==Crystal structure of (S)-3-hydroxybutyryl-CoA dehydrogenase PaaH1 in complex with acetoacetyl-CoA==
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<StructureSection load='4pze' size='340' side='right' caption='[[4pze]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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<StructureSection load='4pze' size='340' side='right'caption='[[4pze]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4pze]] is a 9 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PZE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4pze]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_necator_H16 Cupriavidus necator H16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PZE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pzc|4pzc]], [[4pzd|4pzd]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAA:ACETOACETYL-COENZYME+A'>CAA</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxyacyl-CoA_dehydrogenase 3-hydroxyacyl-CoA dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.35 1.1.1.35] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pze OCA], [https://pdbe.org/4pze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pze RCSB], [https://www.ebi.ac.uk/pdbsum/4pze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pze ProSAT]</span></td></tr>
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<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=4pze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pze OCA], [http://pdbe.org/4pze PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pze RCSB], [http://www.ebi.ac.uk/pdbsum/4pze PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pze ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q0KEY8_CUPNH Q0KEY8_CUPNH]
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3-Hydroxybutyryl-CoA dehydrogenase is an enzyme involved in the synthesis of the biofuel n-butanol by converting acetoacetyl-CoA to 3-hydroxybutyryl-CoA. To investigate the molecular mechanism of n-butanol biosynthesis, we determined crystal structures of the Ralstonia eutropha-derived 3-hydroxybutyryl-CoA dehydrogenase (RePaaH1) in complex with either its cofactor NAD(+) or its substrate acetoacetyl-CoA. While the biologically active structure is dimeric, the monomer of RePaaH1 comprises two separated domains with an N-terminal Rossmann fold and a C-terminal helical bundle for dimerization. In this study, we show that the cofactor-binding site is located on the Rossmann fold and is surrounded by five loops and one helix. The binding mode of the acetoacetyl-CoA substrate was found to be that the adenosine diphosphate moiety is not highly stabilized compared with the remainder of the molecule. Residues involved in catalysis and substrate binding were further confirmed by site-directed mutagenesis experiments, and kinetic properties of RePaaH1were examined as well. Our findings contribute to the understanding of 3-hydroxybutyryl-CoA dehydrogenase catalysis, and will be useful in enhancing the efficiency of n-butanol biosynthesis by structure based protein engineering.
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Crystal structure and biochemical properties of the (S)-3-hydroxybutyryl-CoA dehydrogenase PaaH1 from Ralstonia eutropha.,Kim J, Chang JH, Kim KJ Biochem Biophys Res Commun. 2014 May 30;448(2):163-8. doi:, 10.1016/j.bbrc.2014.04.101. Epub 2014 Apr 29. PMID:24792376<ref>PMID:24792376</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4pze" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: 3-hydroxyacyl-CoA dehydrogenase]]
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[[Category: Cupriavidus necator H16]]
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[[Category: Chang, J H]]
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[[Category: Large Structures]]
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[[Category: Kim, J]]
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[[Category: Chang JH]]
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[[Category: Kim, K J]]
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[[Category: Kim J]]
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[[Category: Oxidoreductase]]
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[[Category: Kim KJ]]
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[[Category: Rossmann fold]]
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Current revision

Crystal structure of (S)-3-hydroxybutyryl-CoA dehydrogenase PaaH1 in complex with acetoacetyl-CoA

PDB ID 4pze

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