8qhf: Difference between revisions
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==Corynebacterium glutamicum mycoloyltransferase C acyl-enzyme intermediate== | |||
<StructureSection load='8qhf' size='340' side='right'caption='[[8qhf]], [[Resolution|resolution]] 2.69Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8qhf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QHF 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]] 2.69Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900006:trehalose'>PRD_900006</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=VBL:(2~{S},3~{R})-2-pentyloctane-1,3-diol'>VBL</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=8qhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qhf OCA], [https://pdbe.org/8qhf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qhf RCSB], [https://www.ebi.ac.uk/pdbsum/8qhf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qhf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8NTG4_CORGL Q8NTG4_CORGL] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein mycoloylation is a newly characterized post-translational modification (PTM) specifically found in Corynebacteriales, an order of bacteria that includes numerous human pathogens. Their envelope is composed of a unique outer membrane, the so-called mycomembrane made of very-long chain fatty acids, named mycolic acids. Recently, some mycomembrane proteins including PorA have been unambiguously shown to be covalently modified with mycolic acids in the model organism Corynebacterium glutamicum by a mechanism that relies on the mycoloyltransferase MytC. This PTM represents the first example of protein O-acylation in prokaryotes and the first example of protein modification by mycolic acid. Through the design and synthesis of trehalose monomycolate (TMM) analogs, we prove that i) MytC is the mycoloyltransferase directly involved in this PTM, ii) TMM, but not trehalose dimycolate (TDM), is a suitable mycolate donor for PorA mycoloylation, iii) MytC is able to discriminate between an acyl and a mycoloyl chain in vitro unlike other trehalose mycoloyltransferases. We also solved the structure of MytC acyl-enzyme obtained with a soluble short TMM analogs which constitutes the first mycoloyltransferase structure with a covalently linked to an authentic mycolic acid moiety. These data highlight the great conformational flexibility of the active site of MytC during the reaction cycle and pave the way for a better understanding of the catalytic mechanism of all members of the mycoloyltransferase family including the essential Antigen85 enzymes in Mycobacteria. | |||
Synthetic mycolates derivatives to decipher protein mycoloylation, a unique post-translational modification in bacteria.,Lesur E, Zhang Y, Dautin N, Dietrich C, Li de la Sierra-Gallay I, Augusto LA, Rollando P, Lazar N, Urban D, Doisneau G, Constantinesco-Becker F, Van Tilbeurgh H, Guianvarc'h D, Bourdreux Y, Bayan N J Biol Chem. 2025 Jan 27:108243. doi: 10.1016/j.jbc.2025.108243. PMID:39880088<ref>PMID:39880088</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Lesur | <div class="pdbe-citations 8qhf" style="background-color:#fffaf0;"></div> | ||
[[Category: Li | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Corynebacterium glutamicum]] | |||
[[Category: Large Structures]] | |||
[[Category: Lesur E]] | |||
[[Category: Li de la Sierra-Gallay I]] | |||
Latest revision as of 09:14, 12 February 2025
Corynebacterium glutamicum mycoloyltransferase C acyl-enzyme intermediateCorynebacterium glutamicum mycoloyltransferase C acyl-enzyme intermediate
Structural highlights
FunctionPublication Abstract from PubMedProtein mycoloylation is a newly characterized post-translational modification (PTM) specifically found in Corynebacteriales, an order of bacteria that includes numerous human pathogens. Their envelope is composed of a unique outer membrane, the so-called mycomembrane made of very-long chain fatty acids, named mycolic acids. Recently, some mycomembrane proteins including PorA have been unambiguously shown to be covalently modified with mycolic acids in the model organism Corynebacterium glutamicum by a mechanism that relies on the mycoloyltransferase MytC. This PTM represents the first example of protein O-acylation in prokaryotes and the first example of protein modification by mycolic acid. Through the design and synthesis of trehalose monomycolate (TMM) analogs, we prove that i) MytC is the mycoloyltransferase directly involved in this PTM, ii) TMM, but not trehalose dimycolate (TDM), is a suitable mycolate donor for PorA mycoloylation, iii) MytC is able to discriminate between an acyl and a mycoloyl chain in vitro unlike other trehalose mycoloyltransferases. We also solved the structure of MytC acyl-enzyme obtained with a soluble short TMM analogs which constitutes the first mycoloyltransferase structure with a covalently linked to an authentic mycolic acid moiety. These data highlight the great conformational flexibility of the active site of MytC during the reaction cycle and pave the way for a better understanding of the catalytic mechanism of all members of the mycoloyltransferase family including the essential Antigen85 enzymes in Mycobacteria. Synthetic mycolates derivatives to decipher protein mycoloylation, a unique post-translational modification in bacteria.,Lesur E, Zhang Y, Dautin N, Dietrich C, Li de la Sierra-Gallay I, Augusto LA, Rollando P, Lazar N, Urban D, Doisneau G, Constantinesco-Becker F, Van Tilbeurgh H, Guianvarc'h D, Bourdreux Y, Bayan N J Biol Chem. 2025 Jan 27:108243. doi: 10.1016/j.jbc.2025.108243. PMID:39880088[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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