3sj7

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

Structural highlights 3sj7 is a 2 chain structure with sequence from Staa8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , Gene: SAOUHSC_01199 (STAA8) Activity: [acyl-carrier-protein_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number 1.1.1.100 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 3sj7, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image