Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dutta D, Bhattacharyya S, Das AK. Crystal structure and fluorescence studies reveal the role of helical dimeric interface of staphylococcal FabG1 in positive cooperativity for NADPH. Proteins. 2012 Jan 9. doi: 10.1002/prot.24024. PMID:22275129 doi:10.1002/prot.24024
