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| | <StructureSection load='5flg' size='340' side='right'caption='[[5flg]], [[Resolution|resolution]] 2.04Å' scene=''> | | <StructureSection load='5flg' size='340' side='right'caption='[[5flg]], [[Resolution|resolution]] 2.04Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5flg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FLG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FLG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5flg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FLG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PML:PIMELIC+ACID'>PML</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]] 2.04Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fll|5fll]], [[5fm0|5fm0]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PML:PIMELIC+ACID'>PML</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/6-carboxyhexanoate--CoA_ligase 6-carboxyhexanoate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.14 6.2.1.14] </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=5flg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5flg OCA], [https://pdbe.org/5flg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5flg RCSB], [https://www.ebi.ac.uk/pdbsum/5flg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5flg 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=5flg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5flg OCA], [http://pdbe.org/5flg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5flg RCSB], [http://www.ebi.ac.uk/pdbsum/5flg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5flg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BIOW_BACSU BIOW_BACSU]] Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP. | + | [https://www.uniprot.org/uniprot/BIOW_BACSU BIOW_BACSU] Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP. |
| | <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: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: 6-carboxyhexanoate--CoA ligase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Campopiano, D J]] | + | [[Category: Campopiano DJ]] |
| - | [[Category: Moynie, L]] | + | [[Category: Moynie L]] |
| - | [[Category: Naismith, J H]] | + | [[Category: Naismith JH]] |
| - | [[Category: Wang, M]] | + | [[Category: Wang M]] |
| - | [[Category: Ligase]]
| + | |
| Structural highlights
Function
BIOW_BACSU Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.
Publication Abstract from PubMed
Biotin is an essential vitamin in plants and mammals, functioning as the carbon dioxide carrier within central lipid metabolism. Bacterial pimeloyl-CoA synthetase (BioW) acts as a highly specific substrate-selection gate, ensuring the integrity of the carbon chain in biotin synthesis. BioW catalyzes the condensation of pimelic acid (C7 dicarboxylic acid) with CoASH in an ATP-dependent manner to form pimeloyl-CoA, the first dedicated biotin building block. Multiple structures of Bacillus subtilis BioW together capture all three substrates, as well as the intermediate pimeloyl-adenylate and product pyrophosphate (PPi), indicating that the enzyme uses an internal ruler to select the correct dicarboxylic acid substrate. Both the catalytic mechanism and the surprising stability of the adenylate intermediate were rationalized through site-directed mutagenesis. Building on this understanding, BioW was engineered to synthesize high-value heptanoyl (C7) and octanoyl (C8) monocarboxylic acid-CoA and C8 dicarboxylic-CoA products, highlighting the enzyme's synthetic potential.
Using the pimeloyl-CoA synthetase adenylation fold to synthesize fatty acid thioesters.,Wang M, Moynie L, Harrison PJ, Kelly V, Piper A, Naismith JH, Campopiano DJ Nat Chem Biol. 2017 Apr 17. doi: 10.1038/nchembio.2361. PMID:28414710[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang M, Moynie L, Harrison PJ, Kelly V, Piper A, Naismith JH, Campopiano DJ. Using the pimeloyl-CoA synthetase adenylation fold to synthesize fatty acid thioesters. Nat Chem Biol. 2017 Apr 17. doi: 10.1038/nchembio.2361. PMID:28414710 doi:http://dx.doi.org/10.1038/nchembio.2361
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