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| | <StructureSection load='7cw5' size='340' side='right'caption='[[7cw5]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='7cw5' size='340' side='right'caption='[[7cw5]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7cw5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baccr Baccr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CW5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7CW5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7cw5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CW5 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></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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BC_5344 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226900 BACCR])</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></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acetyltransferase Acetyl-CoA C-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.9 2.3.1.9] </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=7cw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cw5 OCA], [https://pdbe.org/7cw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cw5 RCSB], [https://www.ebi.ac.uk/pdbsum/7cw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cw5 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=7cw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cw5 OCA], [http://pdbe.org/7cw5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7cw5 RCSB], [http://www.ebi.ac.uk/pdbsum/7cw5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7cw5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q814S6_BACCR Q814S6_BACCR] |
| | <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: Acetyl-CoA C-acetyltransferase]] | + | [[Category: Bacillus cereus ATCC 14579]] |
| - | [[Category: Baccr]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hong, J]] | + | [[Category: Hong J]] |
| - | [[Category: Kim, K J]] | + | [[Category: Kim KJ]] |
| - | [[Category: Acetyl-coa acetyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q814S6_BACCR
Publication Abstract from PubMed
Bacillus cereus ATCC 14579 is a known polyhydroxybutyrate (PHB)-producing microorganism that possesses genes associated with PHB synthesis such as PhaA, PhaB, and PHA synthases. PhaA (i.e., thiolase) is the first enzyme in the PHA biosynthetic pathway, which catalyze the condensation of two acetyl-CoA molecules to acetoacetyl-CoA. Our study elucidated the crystal structure of PhaA in Bacillus cereus ATCC 14579 (BcTHL) in its apo- and CoA-bound forms. BcTHL adopts a type II biosynthetic thiolase structure by forming a tetramer. The crystal structure of CoA-complexed BcTHL revealed that the substrate binding site of BcTHL is constituted by different residues compared with other known thiolases. Our study also revealed that Arg221, a residue involved in ADP binding, undergoes a positional conformational change upon the binding of the CoA molecule.
Crystal structure of an acetyl-CoA acetyltransferase from PHB producing bacterium Bacillus cereus ATCC 14579.,Hong J, Park W, Seo H, Kim IK, Kim KJ Biochem Biophys Res Commun. 2020 Sep 21. pii: S0006-291X(20)31789-7. doi:, 10.1016/j.bbrc.2020.09.048. PMID:32972748[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hong J, Park W, Seo H, Kim IK, Kim KJ. Crystal structure of an acetyl-CoA acetyltransferase from PHB producing bacterium Bacillus cereus ATCC 14579. Biochem Biophys Res Commun. 2020 Sep 21. pii: S0006-291X(20)31789-7. doi:, 10.1016/j.bbrc.2020.09.048. PMID:32972748 doi:http://dx.doi.org/10.1016/j.bbrc.2020.09.048
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