5tva

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<StructureSection load='5tva' size='340' side='right'caption='[[5tva]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='5tva' size='340' side='right'caption='[[5tva]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5tva]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TVA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TVA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5tva]] 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=5TVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TVA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tv5|5tv5]], [[5tv6|5tv6]], [[5tv8|5tv8]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5tva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tva OCA], [https://pdbe.org/5tva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tva RCSB], [https://www.ebi.ac.uk/pdbsum/5tva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tva ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5tva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tva OCA], [http://pdbe.org/5tva PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tva RCSB], [http://www.ebi.ac.uk/pdbsum/5tva PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tva ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/BIOW_AQUAE BIOW_AQUAE]] Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.
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[https://www.uniprot.org/uniprot/BIOW_AQUAE BIOW_AQUAE] Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5tva" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: 6-carboxyhexanoate--CoA ligase]]
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[[Category: Aquifex aeolicus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Agarwal, V]]
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[[Category: Agarwal V]]
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[[Category: Cronan, J E]]
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[[Category: Cronan JE]]
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[[Category: Deveryshetty, J]]
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[[Category: Deveryshetty J]]
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[[Category: Dong, S H]]
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[[Category: Dong S-H]]
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[[Category: Estrada, P]]
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[[Category: Estrada P]]
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[[Category: Manandhar, M]]
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[[Category: Manandhar M]]
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[[Category: Nair, S K]]
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[[Category: Nair SK]]
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[[Category: Adenylation]]
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[[Category: Ligase]]
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[[Category: Pimeloyl-coa ligase]]
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Revision as of 15:43, 6 March 2024

A. aeolicus BioW with AMP and CoA

PDB ID 5tva

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