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| | <StructureSection load='5zai' size='340' side='right'caption='[[5zai]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='5zai' size='340' side='right'caption='[[5zai]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5zai]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Mets5 Mets5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZAI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZAI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zai]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Metallosphaera_sedula_DSM_5348 Metallosphaera sedula DSM 5348]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZAI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Msed_2001 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=399549 METS5])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxypropionyl-CoA_dehydratase 3-hydroxypropionyl-CoA dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.116 4.2.1.116] </span></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=5zai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zai OCA], [https://pdbe.org/5zai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zai RCSB], [https://www.ebi.ac.uk/pdbsum/5zai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zai ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zai OCA], [http://pdbe.org/5zai PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zai RCSB], [http://www.ebi.ac.uk/pdbsum/5zai PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zai ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HPCD_METS5 HPCD_METS5]] Plays a role in autotrophic carbon fixation via the 3-hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the reversible dehydration of 3-hydroxypropionyl-CoA to form acryloyl-CoA, and the reversible dehydration of (S)-3-hydroxybutyryl-CoA to form crotonyl-CoA. Inactive towards (R)-3-hydroxybutyryl-CoA.<ref>PMID:19429610</ref> | + | [https://www.uniprot.org/uniprot/HPCD_METS5 HPCD_METS5] Plays a role in autotrophic carbon fixation via the 3-hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the reversible dehydration of 3-hydroxypropionyl-CoA to form acryloyl-CoA, and the reversible dehydration of (S)-3-hydroxybutyryl-CoA to form crotonyl-CoA. Inactive towards (R)-3-hydroxybutyryl-CoA.<ref>PMID:19429610</ref> |
| | <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-hydroxypropionyl-CoA dehydratase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mets5]] | + | [[Category: Metallosphaera sedula DSM 5348]] |
| - | [[Category: Kim, K J]] | + | [[Category: Kim KJ]] |
| - | [[Category: Lee, D]] | + | [[Category: Lee D]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
HPCD_METS5 Plays a role in autotrophic carbon fixation via the 3-hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the reversible dehydration of 3-hydroxypropionyl-CoA to form acryloyl-CoA, and the reversible dehydration of (S)-3-hydroxybutyryl-CoA to form crotonyl-CoA. Inactive towards (R)-3-hydroxybutyryl-CoA.[1]
Publication Abstract from PubMed
Metallosphaera sedula is a thermoacidophilic autotrophic archaeon known to utilize the 3-hydroxypropionate/4-hydroxybutyrate cycle (3-HP/4-HB cycle) as carbon fixation pathway. 3-Hydroxypropionyl-CoA dehydratase (3HPCD) is an enzyme involved in the 3-HP/4-HB cycle by converting 3-hydroxypropionyl-CoA to acryloyl-CoA. To elucidate the molecular mechanism of 3HPCD from M. sedula (Ms3HPCD), we determined its crystal structure in complex with Coenzyme A (CoA). Ms3HPCD showed an overall structure and the CoA-binding mode similar to other enoyl-CoA hydratase (ECH) family enzymes. However, compared with the other ECHs, Ms3HPCD has a tightly formed alpha3 helix near the active site, and bulky aromatic residues are located at the enoyl-group binding site, resulting in the enzyme having an optimal substrate binding site for accepting short-chain 3-hydroxyacyl-CoA as a substrate. Moreover, based on the phylogenetic tree analysis, we propose that the 3HPCD homologues from the phylum Crenarchaeota have an enoyl-group binding pocket similar to that of bacterial short-chain ECHs.
Structural Insight into Substrate Specificity of 3-Hydroxypropionyl-Coenzyme A Dehydratase from Metallosphaera sedula.,Lee D, Kim KJ Sci Rep. 2018 Jul 16;8(1):10692. doi: 10.1038/s41598-018-29070-w. PMID:30013155[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Teufel R, Kung JW, Kockelkorn D, Alber BE, Fuchs G. 3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales. J Bacteriol. 2009 Jul;191(14):4572-81. doi: 10.1128/JB.00068-09. Epub 2009 May 8. PMID:19429610 doi:http://dx.doi.org/10.1128/JB.00068-09
- ↑ Lee D, Kim KJ. Structural Insight into Substrate Specificity of 3-Hydroxypropionyl-Coenzyme A Dehydratase from Metallosphaera sedula. Sci Rep. 2018 Jul 16;8(1):10692. doi: 10.1038/s41598-018-29070-w. PMID:30013155 doi:http://dx.doi.org/10.1038/s41598-018-29070-w
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