2FAC

Crystal structure of E. coli hexanoyl-ACP

Summary for 2FAC

• Entry DOI: 10.2210/pdb2fac/pdb
• Related: 1L0H 1L0I
• Descriptor: Acyl carrier protein, ZINC ION, S-(2-{[N-(2-HYDROXY-4-{[HYDROXY(OXIDO)PHOSPHINO]OXY}-3,3-DIMETHYLBUTANOYL)-BETA-ALANYL]AMINO}ETHYL) HEXANETHIOATE, ... (4 entities in total)
• Functional Keywords: acyl carrier protein, acyl chain binding, fatty acid biosynthesis, biosynthetic protein
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A6A8
• Total number of polymer chains: 2
• Total formula weight: 18629.01

Authors

Roujeinikova, A. (deposition date: 2005-12-07, release date: 2006-09-26, Last modification date: 2024-11-20)

Primary citation

Roujeinikova, A.,Simon, W.J.,Gilroy, J.,Rice, D.W.,Rafferty, J.B.,Slabas, A.R.
Structural Studies of Fatty Acyl-(Acyl Carrier Protein) Thioesters Reveal a Hydrophobic Binding Cavity that Can Expand to Fit Longer Substrates.
J.Mol.Biol., 365:135-145, 2007

PubMed Abstract: 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.

PubMed: 17059829
DOI: 10.1016/j.jmb.2006.09.049

Experimental method

X-RAY DIFFRACTION (1.76 Å)