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3sj7
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| - | [[ | + | ==Structure of beta-ketoacetyl-CoA reductase (FabG) from Staphylococcus aureus complex with NADPH== |
| + | <StructureSection load='3sj7' size='340' side='right' caption='[[3sj7]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3sj7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus Staphylococcus aureus subsp. aureus]. 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> | ||
| + | </td></tr><tr><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><br> | ||
| + | <tr><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=46170 Staphylococcus aureus subsp. aureus])</td></tr> | ||
| + | <tr><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> | ||
| + | <tr><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://www.rcsb.org/pdb/explore.do?structureId=3sj7 RCSB], [http://www.ebi.ac.uk/pdbsum/3sj7 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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| - | == | + | |
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[[Category: Staphylococcus aureus subsp. aureus]] | [[Category: Staphylococcus aureus subsp. aureus]] | ||
[[Category: Bhattacharyya, S.]] | [[Category: Bhattacharyya, S.]] | ||
Revision as of 05:24, 5 June 2014
Structure of beta-ketoacetyl-CoA reductase (FabG) from Staphylococcus aureus complex with NADPH
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