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| | <StructureSection load='5tv5' size='340' side='right'caption='[[5tv5]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5tv5' size='340' side='right'caption='[[5tv5]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5tv5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TV5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TV5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5tv5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TV5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TV5 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tv6|5tv6]], [[5tv8|5tv8]], [[5tva|5tva]]</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]] 2.5Å</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=5tv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tv5 OCA], [https://pdbe.org/5tv5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tv5 RCSB], [https://www.ebi.ac.uk/pdbsum/5tv5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tv5 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=5tv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tv5 OCA], [http://pdbe.org/5tv5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tv5 RCSB], [http://www.ebi.ac.uk/pdbsum/5tv5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tv5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BIOW_AQUAE BIOW_AQUAE]] Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP. | + | [https://www.uniprot.org/uniprot/BIOW_AQUAE BIOW_AQUAE] Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Reactions that activate carboxylates through acyl-adenylate intermediates are found throughout biology and include acyl- and aryl-CoA synthetases and tRNA synthetases. Here we describe the characterization of Aquifex aeolicus BioW, which represents a new protein fold within the superfamily of adenylating enzymes. Substrate-bound structures identified the enzyme active site and elucidated the mechanistic strategy for conjugating CoA to the seven-carbon alpha,omega-dicarboxylate pimelate, a biotin precursor. Proper position of reactive groups for the two half-reactions is achieved solely through movements of active site residues, as confirmed by site-directed mutational analysis. The ability of BioW to hydrolyze adenylates of noncognate substrates is reminiscent of pre-transfer proofreading observed in some tRNA synthetases, and we show that this activity can be abolished by mutation of a single residue. These studies illustrate how BioW can carry out three different biologically prevalent chemical reactions (adenylation, thioesterification, and proofreading) in the context of a new protein fold.
| + | |
| - | | + | |
| - | The pimeloyl-CoA synthetase BioW defines a new fold for adenylate-forming enzymes.,Estrada P, Manandhar M, Dong SH, Deveryshetty J, Agarwal V, Cronan JE, Nair SK Nat Chem Biol. 2017 Apr 17. doi: 10.1038/nchembio.2359. PMID:28414711<ref>PMID:28414711</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5tv5" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 6-carboxyhexanoate--CoA ligase]] | + | [[Category: Aquifex aeolicus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Agarwal, V]] | + | [[Category: Agarwal V]] |
| - | [[Category: Cronan, J E]] | + | [[Category: Cronan JE]] |
| - | [[Category: Deveryshetty, J]] | + | [[Category: Deveryshetty J]] |
| - | [[Category: Dong, S H]] | + | [[Category: Dong S-H]] |
| - | [[Category: Estrada, P]] | + | [[Category: Estrada P]] |
| - | [[Category: Manandhar, M]] | + | [[Category: Manandhar M]] |
| - | [[Category: Nair, S K]] | + | [[Category: Nair SK]] |
| - | [[Category: Adenylation]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Pimeloyl-coa ligase]]
| + | |
