3sj7

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==Structure of beta-ketoacetyl-CoA reductase (FabG) from Staphylococcus aureus complex with NADPH==
==Structure of beta-ketoacetyl-CoA reductase (FabG) from Staphylococcus aureus complex with NADPH==
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<StructureSection load='3sj7' size='340' side='right' caption='[[3sj7]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='3sj7' size='340' side='right'caption='[[3sj7]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sj7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SJ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SJ7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3sj7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SJ7 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=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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]] 2.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAOUHSC_01199 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93061 STAA8])</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=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </span></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=3sj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sj7 OCA], [https://pdbe.org/3sj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sj7 RCSB], [https://www.ebi.ac.uk/pdbsum/3sj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sj7 ProSAT]</span></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=3sj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sj7 OCA], [http://pdbe.org/3sj7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sj7 RCSB], [http://www.ebi.ac.uk/pdbsum/3sj7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sj7 ProSAT]</span></td></tr>
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</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/Q2FZ53_STAA8 Q2FZ53_STAA8]
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Crystal structure of Staphylococcal beta-ketoacyl-ACP reductase 1 (SaFabG1) complexed with NADPH is determined at 2.5 A resolution. The enzyme is essential in FAS-II pathway and utilizes NADPH to reduce beta-ketoacyl-ACP to (S)-beta-hydroxyacyl-ACP. Unlike the tetrameric FabGs, dimeric SaFabG1 shows positive homotropic cooperativity towards NADPH. Analysis of FabG:NADPH binary crystal structure endorses that NADPH interacts directly with the helices alpha4 and alpha5 those are present on a dimerization interface. A steady shift in tryptophan (of alpha4 helix) emission peak upon steady increment of NADPH concentration reveals that the dimeric interface is formed by alpha4-alpha4' and alpha5-alpha5' helices. This dimeric interface imparts positive homotropic cooperativity towards NADPH. PEG, a substrate mimicking molecule is also found near the active site of the enzyme. Proteins 2012. (c) 2012 Wiley-Liss, Inc.
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Crystal structure and fluorescence studies reveal the role of helical dimeric interface of staphylococcal FabG1 in positive cooperativity for NADPH.,Dutta D, Bhattacharyya S, Das AK Proteins. 2012 Jan 9. doi: 10.1002/prot.24024. PMID:22275129<ref>PMID:22275129</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 3sj7" 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: Staa8]]
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[[Category: Large Structures]]
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[[Category: Bhattacharyya, S]]
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[[Category: Staphylococcus aureus subsp. aureus NCTC 8325]]
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[[Category: Das, A K]]
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[[Category: Bhattacharyya S]]
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[[Category: Dutta, D]]
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[[Category: Das AK]]
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[[Category: Ketoreductase]]
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[[Category: Dutta D]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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Current revision

Structure of beta-ketoacetyl-CoA reductase (FabG) from Staphylococcus aureus complex with NADPH

PDB ID 3sj7

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