1L0I

Crystal structure of butyryl-ACP I62M mutant

Summary for 1L0I

• Entry DOI: 10.2210/pdb1l0i/pdb
• Related: 1L0H
• Descriptor: Acyl carrier protein, SODIUM ION, ZINC ION, ... (6 entities in total)
• Functional Keywords: acyl carrier protein, acyl chain binding, fatty acid biosynthesis, lipid transport
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A6A8
• Total number of polymer chains: 1
• Total formula weight: 9709.78

Authors

Roujeinikova, A.,Baldock, C.,Simon, W.J.,Gilroy, J.,Baker, P.J.,Stuitje, A.R.,Rice, D.W.,Slabas, A.R.,Rafferty, J.B. (deposition date: 2002-02-11, release date: 2003-02-11, Last modification date: 2024-10-30)

Primary citation

Roujeinikova, A.,Baldock, C.,Simon, W.J.,Gilroy, J.,Baker, P.J.,Stuitje, A.R.,Rice, D.W.,Slabas, A.R.,Rafferty, J.B.
X-ray Crystallographic Studies on Butyryl-ACP Reveal Flexibility of the Structure around a Putative Acyl Chain Binding Site
Structure, 10:825-835, 2002

PubMed Abstract: Acyl carrier protein (ACP) is an essential cofactor in biosynthesis of fatty acids and many other reactions that require acyl transfer steps. We have determined the first crystal structures of an acylated form of ACP from E. coli, that of butyryl-ACP. Our analysis of the molecular surface of ACP reveals a plastic hydrophobic cavity in the vicinity of the phosphopantethylated Ser36 residue that is expanded and occupied by the butyryl and beta-mercaptoethylamine moieties of the acylated 4'-phosphopantetheine group in one of our crystal forms. In the other form, the cavity is contracted, and we propose that the protein has adopted the conformation after delivery of substrate into the active site of a partner enzyme.

PubMed: 12057197
DOI: 10.1016/S0969-2126(02)00775-X

Experimental method

X-RAY DIFFRACTION (1.2 Å)