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5ey8
From Proteopedia
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==Structure of FadD32 from Mycobacterium smegmatis complexed to AMPC20== | ==Structure of FadD32 from Mycobacterium smegmatis complexed to AMPC20== | ||
<StructureSection load='5ey8' size='340' side='right' caption='[[5ey8]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='5ey8' size='340' side='right' caption='[[5ey8]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
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<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=5ey8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ey8 OCA], [http://pdbe.org/5ey8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ey8 RCSB], [http://www.ebi.ac.uk/pdbsum/5ey8 PDBsum]</span></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=5ey8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ey8 OCA], [http://pdbe.org/5ey8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ey8 RCSB], [http://www.ebi.ac.uk/pdbsum/5ey8 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mycolic acids are essential components of the mycobacterial cell envelope, and their biosynthetic pathway is one of the targets of first-line antituberculous drugs. This pathway contains a number of potential targets, including some that have been identified only recently and have yet to be explored. One such target, FadD32, is required for activation of the long meromycolic chain and is essential for mycobacterial growth. We report here an in-depth biochemical, biophysical, and structural characterization of four FadD32 orthologs, including the very homologous enzymes fromMycobacterium tuberculosisandMycobacterium marinum Determination of the structures of two complexes with alkyl adenylate inhibitors has provided direct information, with unprecedented detail, about the active site of the enzyme and the associated hydrophobic tunnel, shedding new light on structure-function relationships and inhibition mechanisms by alkyl adenylates and diarylated coumarins. This work should pave the way for the rational design of inhibitors of FadD32, a highly promising drug target. | ||
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| + | Insight into Structure-Function Relationships and Inhibition of the Fatty Acyl-AMP Ligase (FadD32) Orthologs from Mycobacteria.,Guillet V, Galandrin S, Maveyraud L, Ladeveze S, Mariaule V, Bon C, Eynard N, Daffe M, Marrakchi H, Mourey L J Biol Chem. 2016 Apr 8;291(15):7973-89. doi: 10.1074/jbc.M115.712612. Epub 2016 , Feb 21. PMID:26900152<ref>PMID:26900152</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5ey8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 18:45, 10 May 2016
Structure of FadD32 from Mycobacterium smegmatis complexed to AMPC20
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