6rcx

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==Mycobacterial 4'-phosphopantetheinyl transferase PptAb in complex with the ACP domain of PpsC.==
==Mycobacterial 4'-phosphopantetheinyl transferase PptAb in complex with the ACP domain of PpsC.==
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<StructureSection load='6rcx' size='340' side='right'caption='[[6rcx]]' scene=''>
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<StructureSection load='6rcx' size='340' side='right'caption='[[6rcx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RCX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RCX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6rcx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myca9 Myca9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RCX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RCX FirstGlance]. <br>
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</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=6rcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rcx OCA], [http://pdbe.org/6rcx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rcx RCSB], [http://www.ebi.ac.uk/pdbsum/6rcx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rcx ProSAT]</span></td></tr>
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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=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qwu|6qwu]], [[6qxq|6qxq]], [[6qxr|6qxr]], [[6qyf|6qyf]], [[6qyg|6qyg]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAB_3117c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=561007 MYCA9]), ppsC, Rv2933 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=561007 MYCA9])</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/Beta-ketoacyl-[acyl-carrier-protein]_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </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=6rcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rcx OCA], [http://pdbe.org/6rcx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rcx RCSB], [http://www.ebi.ac.uk/pdbsum/6rcx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rcx ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/PPSC_MYCTU PPSC_MYCTU]] Involved in the elongation of either C22-24 fatty acids by the addition of malonyl-CoA and methylmalonyl-CoA extender units to yield phthiocerol derivatives.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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One central question surrounding the biosynthesis of fatty acids and polyketide-derived natural products is how the 4'-phosphopantetheinyl transferase (PPTase) interrogates the essential acyl carrier protein (ACP) domain to fulfill the initial activation step. The triggering factor of this study was the lack of structural information on PPTases at physiological pH, which could bias our comprehension of the mechanism of action of these important enzymes. Structural and functional studies on the family II PPTase PptAb of Mycobacterium abscessus show that pH has a profound effect on the coordination of metal ions and on the conformation of endogenously bound coenzyme A (CoA). The observed conformational flexibility of CoA at physiological pH is accompanied by a disordered 4'-phosphopantetheine (Ppant) moiety. Finally, structural and dynamical information on an isolated mycobacterial ACP domain, in its apo form and in complex with the activator PptAb, suggests an alternate mechanism for the post-translational modification of modular megasynthases.
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Conformational flexibility of coenzyme A and its impact on the post-translational modification of acyl carrier proteins by 4'-phosphopantetheinyl transferases.,Nguyen MC, Saurel O, Carivenc C, Gavalda S, Saitta S, Tran MP, Milon A, Chalut C, Guilhot C, Mourey L, Pedelacq JD FEBS J. 2020 Mar 3. doi: 10.1111/febs.15273. PMID:32128972<ref>PMID:32128972</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 6rcx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Mourey L]]
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[[Category: Myca9]]
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[[Category: Nguyen MC]]
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[[Category: Mourey, L]]
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[[Category: Pedelacq JD]]
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[[Category: Nguyen, M C]]
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[[Category: Pedelacq, J D]]
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[[Category: Transferase-transport protein complex]]
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[[Category: Transferase/transport protein]]

Revision as of 08:08, 11 November 2020

Mycobacterial 4'-phosphopantetheinyl transferase PptAb in complex with the ACP domain of PpsC.

PDB ID 6rcx

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