View source for 5ey8


==Structure of FadD32 from Mycobacterium smegmatis complexed to AMPC20==
<StructureSection load='5ey8' size='340' side='right'caption='[[5ey8]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ey8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EY8 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]] 3.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5SV:[(2~{R},3~{S},4~{R},5~{R})-5-(6-AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHYL+ICOSYL+HYDROGEN+PHOSPHATE'>5SV</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5ey8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ey8 OCA], [https://pdbe.org/5ey8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ey8 RCSB], [https://www.ebi.ac.uk/pdbsum/5ey8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ey8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FAA32_MYCS2 FAA32_MYCS2] Involved in the biosynthesis of mycolic acids (By similarity). Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the polyketide synthase Pks13 for further chain extension (By similarity). Can use decanoate (C10), dodecanoate (C12) and tetradecanoate (C14) (PubMed:23364516, PubMed:26900152).[UniProtKB:O53580]<ref>PMID:23364516</ref> <ref>PMID:26900152</ref> 
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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mycolicibacterium smegmatis]]
[[Category: Guillet V]]
[[Category: Maveyraud L]]
[[Category: Mourey L]]