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5t2v

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==Crystal structure of MSMEG_6753 a putative betaketoacyl-ACP reductase==
==Crystal structure of MSMEG_6753 a putative betaketoacyl-ACP reductase==
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<StructureSection load='5t2v' size='340' side='right' caption='[[5t2v]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='5t2v' size='340' side='right'caption='[[5t2v]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5t2v]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T2V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T2V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5t2v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T2V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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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=5t2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t2v OCA], [http://pdbe.org/5t2v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t2v RCSB], [http://www.ebi.ac.uk/pdbsum/5t2v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t2v ProSAT]</span></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5t2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t2v OCA], [https://pdbe.org/5t2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t2v RCSB], [https://www.ebi.ac.uk/pdbsum/5t2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t2v ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0R723_MYCS2 A0R723_MYCS2]
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The ketoacyl-acyl carrier protein (ACP) reductase FabG catalyzes the NADPH/NADH dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the fatty acid biosynthesis elongation cycle. FabG proteins are ubiquitous in bacteria and are part of the type II fatty acid synthase system. Mining the Mycobacterium smegmatis genome uncovered several putative FabG-like proteins. Among them, we identified M. smegmatis MSMEG_6753 whose gene was found adjacent to MSMEG_6754, encoding a recently characterized enoyl-CoA dehydratase, and to MSMEG_6755, encoding another potential reductase. Recombinantly expressed and purified MSMEG_6753 exhibits ketoacyl reductase activity in the presence of acetoacetyl-CoA and NADPH. This activity was subsequently confirmed by functional complementation studies in a fabG thermosensitive Escherichia coli mutant. Furthermore, comparison of the apo and the NADP+-bound MSMEG_6753 crystal structures showed that cofactor binding induces a closed conformation of the protein. A DeltaMSMEG_6753 deletion mutant could be generated in M. smegmatis, indicating that this gene is dispensable for mycobacterial growth. Overall, these results showcase the diversity of FabG-like proteins in mycobacteria and new structural features regarding the catalytic mechanism of this important family of enzymes that may be of importance for the rational design of specific FabG inhibitors.
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Binding of NADP+ triggers an open-to-closed transition in a mycobacterial FabG beta-ketoacyl-ACP reductase.,Blaise M, Van Wyk N, Baneres-Roquet F, Guerardel Y, Kremer L Biochem J. 2017 Mar 7;474(6):907-921. doi: 10.1042/BCJ20161052. PMID:28126742<ref>PMID:28126742</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5t2v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baneres-Roquet, F]]
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[[Category: Large Structures]]
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[[Category: Blaise, M]]
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[[Category: Mycolicibacterium smegmatis MC2 155]]
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[[Category: Guerardel, Y]]
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[[Category: Baneres-Roquet F]]
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[[Category: Kremer, L]]
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[[Category: Blaise M]]
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[[Category: Wyk, N Van]]
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[[Category: Guerardel Y]]
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[[Category: Fabg]]
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[[Category: Kremer L]]
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[[Category: Fatty acid]]
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[[Category: Van Wyk N]]
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[[Category: Mycobacterium]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal structure of MSMEG_6753 a putative betaketoacyl-ACP reductase

PDB ID 5t2v

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