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| | <StructureSection load='4pzc' size='340' side='right'caption='[[4pzc]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='4pzc' size='340' side='right'caption='[[4pzc]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pzc]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Alcaligenes_eutropha_h16 Alcaligenes eutropha h16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PZC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pzc]] is a 3 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=4PZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PZC FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pze|4pze]], [[4pzd|4pzd]]</td></tr> | + | </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=4pzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzc OCA], [https://pdbe.org/4pzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pzc RCSB], [https://www.ebi.ac.uk/pdbsum/4pzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzc ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">paaH1, H16_A0282 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=381666 Alcaligenes eutropha H16])</td></tr>
| + | |
| - | <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>
| + | |
| - | <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=4pzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzc OCA], [http://pdbe.org/4pzc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pzc RCSB], [http://www.ebi.ac.uk/pdbsum/4pzc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q0KEY8_CUPNH Q0KEY8_CUPNH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 3-hydroxyacyl-CoA dehydrogenase]] | + | [[Category: Cupriavidus necator H16]] |
| - | [[Category: Alcaligenes eutropha h16]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chang, J H]] | + | [[Category: Chang JH]] |
| - | [[Category: Kim, J]] | + | [[Category: Kim J]] |
| - | [[Category: Kim, K J]] | + | [[Category: Kim KJ]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
Q0KEY8_CUPNH
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim J, Chang JH, Kim KJ. Crystal structure and biochemical properties of the (S)-3-hydroxybutyryl-CoA dehydrogenase PaaH1 from Ralstonia eutropha. 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 doi:http://dx.doi.org/10.1016/j.bbrc.2014.04.101
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