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Solution Structures of Spinach Acyl Carrier Protein with Decanoate and Stearate†
- Publication Year :
- 2006
-
Abstract
- Acyl carrier protein (ACP) is a cofactor in a variety of biosynthetic pathways, including fatty acid metabolism. Thus, it is of interest to determine structures of physiologically relevant ACP-fatty acid complexes. We report here the NMR solution structures of spinach ACP with decanoate (10:0-ACP) and stearate (18:0-ACP) attached to the 4'-phosphopantetheine prosthetic group. The protein in the fatty acid complexes adopts a single conformer, unlike apo- and holo-ACP, which interconvert in solution between two major conformers. The protein component of both 10:0- and 18:0-ACP adopts the four-helix bundle topology characteristic of ACP, and a fatty acid binding cavity was identified in both structures. Portions of the protein close in space to the fatty acid and the 4'-phosphopantetheine were identified using filtered/edited NOESY experiments. A docking protocol was used to generate protein structures containing bound fatty acid for 10:0- and 18:0-ACP. In both cases, the predominant structure contained fatty acid bound down the center of the helical bundle, in agreement with the location of the fatty acid binding pockets. These structures demonstrate the conformational flexibility of spinach ACP and suggest how the protein changes to accommodate its myriad binding partners.
- Subjects :
- Models, Molecular
animal structures
Stereochemistry
Biochemistry
Article
chemistry.chemical_compound
Protein structure
stomatognathic system
Stearate
Spinacia oleracea
Fatty acid binding
Stearates
Acyl Carrier Protein
Serine
Protein Structure, Quaternary
Nuclear Magnetic Resonance, Biomolecular
chemistry.chemical_classification
Binding Sites
biology
Fatty acid metabolism
Decanoates
Fatty acid
humanities
Solutions
Fatty acid synthase
Acyl carrier protein
chemistry
Pantetheine
biology.protein
bacteria
lipids (amino acids, peptides, and proteins)
Phosphopantetheine
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....72343286675a944305fd1c7656acd551