4e1a
From Proteopedia
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| - | [[ | + | ==Phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis at 1.62A resolution== |
| + | <StructureSection load='4e1a' size='340' side='right' caption='[[4e1a]], [[Resolution|resolution]] 1.62Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4e1a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E1A FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">coaD, kdtB, Rv2965c, MT3043, MTCY349.22, u0002e ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pantetheine-phosphate_adenylyltransferase Pantetheine-phosphate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.3 2.7.7.3] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e1a RCSB], [http://www.ebi.ac.uk/pdbsum/4e1a PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Pantetheine-phosphate adenylyltransferase]] | [[Category: Pantetheine-phosphate adenylyltransferase]] | ||
| - | [[Category: Chupova, L A | + | [[Category: Chupova, L A]] |
| - | [[Category: Esipov, R S | + | [[Category: Esipov, R S]] |
| - | [[Category: Kuranova, I P | + | [[Category: Kuranova, I P]] |
| - | [[Category: Smirnova, E A | + | [[Category: Smirnova, E A]] |
| - | [[Category: Timofeev, V I | + | [[Category: Timofeev, V I]] |
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 16:09, 9 December 2014
Phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis at 1.62A resolution
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