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2fad
From Proteopedia
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Crystal structure of E. coli heptanoyl-ACP
Overview
A knowledge of the structures of acyl chain loaded species of the acyl, carrier protein (ACP) as used in fatty acid biosynthesis and a range of, other metabolic events, is essential for a full understanding of the, molecular recognition at the heart of these processes. To date the only, crystal structure of an acylated species of ACP is that of a butyryl, derivative of Escherichia coli ACP. We have now determined the structures, of a family of acylated E. coli ACPs of varying acyl chain length. The, acyl moiety is attached via a thioester bond to a phosphopantetheine, linker that is in turn bound to a serine residue in ACP. The growing acyl, chain can be accommodated within a central cavity in the ACP for transport, during the elongation stages of lipid synthesis through changes in the, conformation of a four alpha-helix bundle. The results not only clarify, the means by which a substrate of varying size and complexity is, transported in the cell but also suggest a mechanism by which interacting, enzymes can recognize the loaded ACP through recognition of surface, features including the conformation of the phosphopantetheine linker.
About this Structure
2FAD is a Single protein structure of sequence from Escherichia coli with NA, ZN and PM5 as ligands. Full crystallographic information is available from OCA.
Reference
Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates., Roujeinikova A, Simon WJ, Gilroy J, Rice DW, Rafferty JB, Slabas AR, J Mol Biol. 2007 Jan 5;365(1):135-45. Epub 2006 Sep 23. PMID:17059829
Page seeded by OCA on Wed Nov 21 10:27:07 2007
