Structural highlights
Function
FABB_ECOLI Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids.
Publication Abstract from PubMed
Fatty acid synthases are dynamic ensembles of enzymes that can biosynthesize long hydrocarbon chains efficiently. Here we visualize the interaction between the Escherichia coli acyl carrier protein (AcpP) and beta-ketoacyl-ACP-synthase I (FabB) using X-ray crystallography, NMR, and molecular dynamics simulations. We leveraged this structural information to alter lipid profiles in vivo and provide a molecular basis for how protein-protein interactions can regulate the fatty acid profile in E. coli.
Molecular basis for interactions between an acyl carrier protein and a ketosynthase.,Milligan JC, Lee DJ, Jackson DR, Schaub AJ, Beld J, Barajas JF, Hale JJ, Luo R, Burkart MD, Tsai SC Nat Chem Biol. 2019 Jul;15(7):669-671. doi: 10.1038/s41589-019-0301-y. Epub 2019 , Jun 17. PMID:31209348[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Milligan JC, Lee DJ, Jackson DR, Schaub AJ, Beld J, Barajas JF, Hale JJ, Luo R, Burkart MD, Tsai SC. Molecular basis for interactions between an acyl carrier protein and a ketosynthase. Nat Chem Biol. 2019 Jul;15(7):669-671. doi: 10.1038/s41589-019-0301-y. Epub 2019 , Jun 17. PMID:31209348 doi:http://dx.doi.org/10.1038/s41589-019-0301-y
