6qyf: Difference between revisions
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<StructureSection load='6qyf' size='340' side='right'caption='[[6qyf]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='6qyf' size='340' side='right'caption='[[6qyf]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == 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 [ | <table><tr><td colspan='2'>[[6qyf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacteroides_abscessus_ATCC_19977 Mycobacteroides abscessus ATCC 19977]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6QYF FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6qyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qyf OCA], [https://pdbe.org/6qyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qyf RCSB], [https://www.ebi.ac.uk/pdbsum/6qyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qyf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/B1MD73_MYCA9 B1MD73_MYCA9] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mycobacteroides abscessus ATCC 19977]] | ||
[[Category: | [[Category: Mourey L]] | ||
[[Category: | [[Category: Nguyen MC]] | ||
[[Category: | [[Category: Pedelacq JD]] | ||
Latest revision as of 15:11, 24 January 2024
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
FunctionPublication 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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