View source for 4h18


==Three dimensional structure of corynomycoloyl tranferase C==
<StructureSection load='4h18' size='340' side='right'caption='[[4h18]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4h18]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum_ATCC_13032 Corynebacterium glutamicum ATCC 13032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H18 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]] 1.755&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=4h18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h18 OCA], [https://pdbe.org/4h18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h18 RCSB], [https://www.ebi.ac.uk/pdbsum/4h18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h18 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8NTG4_CORGL Q8NTG4_CORGL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have previously described the posttranslational modification of pore-forming small proteins of Corynebacterium by mycolic acid, a very-long-chain alpha-alkyl and beta-hydroxy fatty acid. Using a combination of chemical analyses and mass spectrometry, we identified the mycoloyl transferase (Myt) that catalyzes the transfer of the fatty acid residue to yield O-acylated polypeptides. Inactivation of corynomycoloyl transferase C (cg0413 [Corynebacterium glutamicum mytC {CgmytC}]), one of the six Cgmyt genes of C. glutamicum, specifically abolished the O-modification of the pore-forming proteins PorA and PorH, which is critical for their biological activity. Expectedly, complementation of the cg0413 mutant with either the wild-type gene or its orthologues from Corynebacterium diphtheriae and Rhodococcus, but not Nocardia, fully restored the O-acylation of the porins. Consistently, the three-dimensional structure of CgMytC showed the presence of a unique loop that is absent from enzymes that transfer mycoloyl residues onto both trehalose and the cell wall arabinogalactan. These data suggest the implication of this structure in the enzyme specificity for protein instead of carbohydrate.

Identification of a mycoloyl transferase selectively involved in o-acylation of polypeptides in corynebacteriales.,Huc E, de Sousa-D'Auria C, de la Sierra-Gallay IL, Salmeron C, van Tilbeurgh H, Bayan N, Houssin C, Daffe M, Tropis M J Bacteriol. 2013 Sep;195(18):4121-8. doi: 10.1128/JB.00285-13. Epub 2013 Jul 12. PMID:23852866<ref>PMID:23852866</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4h18" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Corynebacterium glutamicum ATCC 13032]]
[[Category: Large Structures]]
[[Category: Bayan N]]
[[Category: Daffe M]]
[[Category: Houssin CH]]
[[Category: Huc E]]
[[Category: Li de la Sierra-Gallay I]]
[[Category: Salmeron CH]]
[[Category: Tropis M]]
[[Category: De Sousa D'Auria C]]
[[Category: Van Tilbeurgh H]]