|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of 3-hydroxyacyl-CoA dehydrogenase from Caenorhadbitis elegans in P1 space group== | | ==Crystal structure of 3-hydroxyacyl-CoA dehydrogenase from Caenorhadbitis elegans in P1 space group== |
| - | <StructureSection load='4j0e' size='340' side='right' caption='[[4j0e]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='4j0e' size='340' side='right'caption='[[4j0e]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4j0e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J0E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J0E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4j0e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J0E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J0E FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j0f|4j0f]]</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=4j0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j0e OCA], [https://pdbe.org/4j0e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j0e RCSB], [https://www.ebi.ac.uk/pdbsum/4j0e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j0e ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">F54C8.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=4j0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j0e OCA], [http://pdbe.org/4j0e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j0e RCSB], [http://www.ebi.ac.uk/pdbsum/4j0e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j0e ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HCDH1_CAEEL HCDH1_CAEEL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 3-hydroxyacyl-CoA dehydrogenase]] | + | [[Category: Caenorhabditis elegans]] |
| - | [[Category: Caeel]] | + | [[Category: Large Structures]] |
| - | [[Category: Sun, F]] | + | [[Category: Sun F]] |
| - | [[Category: Xu, Y]] | + | [[Category: Xu Y]] |
| - | [[Category: Zhai, Y]] | + | [[Category: Zhai Y]] |
| - | [[Category: Dehydrogenase]]
| + | |
| - | [[Category: Fatty acid beta-oxidation]]
| + | |
| - | [[Category: Mitochondrial matrix]]
| + | |
| - | [[Category: Nadh binding]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
HCDH1_CAEEL
Publication Abstract from PubMed
3-Hydroxyacyl-CoA dehydrogenase (HAD; EC 1.1.1.35) is the enzyme that catalyzes the third step in fatty-acid beta-oxidation, oxidizing the hydroxyl group of 3-hydroxyacyl-CoA to a keto group. The 3-hydroxyacyl-CoA dehydrogenase from Caenorhabditis elegans (cHAD) was cloned, overexpressed in Escherichia coli and purified to homogeneity for crystallography. Initial crystals were obtained by the hanging-drop vapour-diffusion method. Optimization of the precipitant concentration and the pH yielded two types of well diffracting crystals with parallelepiped and cuboid shapes, respectively. Complete diffraction data sets were collected and processed from both crystal types. Preliminary crystallographic analysis indicated that the parallelepiped-shaped crystal belonged to space group P1, while the cuboid-shaped crystal belonged to space group P212121. Analyses of computed Matthews coefficient and self-rotation functions suggested that there are two cHAD molecules in one asymmetric unit in both crystals, forming identical dimers but packing in distinct manners.
Purification, crystallization and preliminary crystallographic analysis of 3-hydroxyacyl-CoA dehydrogenase from Caenorhabditis elegans.,Xu Y, Sun F Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May 1;69(Pt 5):515-9. doi:, 10.1107/S1744309113007045. Epub 2013 Apr 30. PMID:23695566[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu Y, Sun F. Purification, crystallization and preliminary crystallographic analysis of 3-hydroxyacyl-CoA dehydrogenase from Caenorhabditis elegans. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May 1;69(Pt 5):515-9. doi:, 10.1107/S1744309113007045. Epub 2013 Apr 30. PMID:23695566 doi:http://dx.doi.org/10.1107/S1744309113007045
|
