3uc5
From Proteopedia
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| - | [[Image:3uc5.png|left|200px]] | ||
| - | + | ==Phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis complexed with ATP== | |
| + | <StructureSection load='3uc5' size='340' side='right'caption='[[3uc5]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3uc5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UC5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></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=3uc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uc5 OCA], [https://pdbe.org/3uc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uc5 RCSB], [https://www.ebi.ac.uk/pdbsum/3uc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uc5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/COAD_MYCTU COAD_MYCTU] Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Structures of recombinant phosphopantetheine adenylyltransferase (PPAT) from Mycobacterium tuberculosis (PPATMt) in the apo form and in complex with the substrate ATP were determined at 1.62 and 1.70 A resolution, respectively, using crystals grown in microgravity by the counter-diffusion method. The ATP molecule of the PPATMt-ATP complex was located with full occupancy in the active-site cavity. Comparison of the solved structures with previously determined structures of PPATMt complexed with the reaction product dephosphocoenzyme A (dPCoA) and the feedback inhibitor coenzyme A (CoA) was performed using superposition on C(alpha) atoms. The peculiarities of the arrangement of the ligands in the active-site cavity of PPATMt are described. The conformational states of the PPAT molecule in the consequent steps of the catalyzed reaction in the apo enzyme and the enzyme-substrate and enzyme-product complexes are characterized. It is shown that the binding of ATP and dPCoA induces the rearrangement of a short part of the polypeptide chain restricting the active-site cavity in the subunits of the hexameric enzyme molecule. The changes in the quaternary structure caused by this rearrangement are accompanied by a variation of the size of the inner water-filled channel which crosses the PPAT molecule along the threefold axis of the hexamer. The molecular mechanism of the observed changes is described. | ||
| - | + | X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis during the catalyzed reaction.,Timofeev V, Smirnova E, Chupova L, Esipov R, Kuranova I Acta Crystallogr D Biol Crystallogr. 2012 Dec;68(Pt 12):1660-70. doi:, 10.1107/S0907444912040206. Epub 2012 Nov 9. PMID:23151631<ref>PMID:23151631</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | <div class="pdbe-citations 3uc5" style="background-color:#fffaf0;"></div> |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
| - | + | [[Category: Chupova LA]] | |
| - | [[Category: Chupova | + | [[Category: Esipov RS]] |
| - | [[Category: Esipov | + | [[Category: Kuranova IP]] |
| - | [[Category: Kuranova | + | [[Category: Smirnova EA]] |
| - | [[Category: Smirnova | + | [[Category: Timofeev VI]] |
| - | [[Category: Timofeev | + | |
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Current revision
Phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis complexed with ATP
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