6qyf: Difference between revisions
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The | ==4'-phosphopantetheinyl transferase PptAb from Mycobacterium abscessus at pH 4.6 with Mg2+ and CoA.== | ||
<StructureSection load='6qyf' size='340' side='right'caption='[[6qyf]], [[Resolution|resolution]] 1.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6qyf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QYF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QYF FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qwu|6qwu]], [[6qxq|6qxq]], [[6qxr|6qxr]], [[6qyg|6qyg]], [[6rcx|6rcx]]</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=6qyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qyf OCA], [http://pdbe.org/6qyf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qyf RCSB], [http://www.ebi.ac.uk/pdbsum/6qyf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qyf ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6qyf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mourey, L]] | [[Category: Mourey, L]] | ||
[[Category: Nguyen, M | [[Category: Nguyen, M C]] | ||
[[Category: Pedelacq, J | [[Category: Pedelacq, J D]] | ||
[[Category: Transferase]] | |||
Revision as of 13:15, 27 March 2020
4'-phosphopantetheinyl transferase PptAb from Mycobacterium abscessus at pH 4.6 with Mg2+ and CoA.4'-phosphopantetheinyl transferase PptAb from Mycobacterium abscessus at pH 4.6 with Mg2+ and CoA.
Structural highlights
Publication Abstract from PubMedOne 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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