STRUCTURAL ANALYSIS OF SPINACH ACYL CARRIER PROTEIN

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The goal of this project is the determine the three dimensional solution structure of spinach acyl carrier protein (ACP) in the apo, holo and acyl forms. A solution structure for E. coli ACP has been reported, however, the structure was completed without using 15N and 13C labeled protein. Additionally, it was reported that the protein interconverts between two structural forms on a 1 second time-scale. Methods have been developed to produce large quantities (350 mg) of 15N and 13C labelled spinach apo-ACP which can then be converted to holo and acyl forms in vitro. By characterizing these three forms by NMR we intend to address the structural changes that occur between each form and also the issue of interconversion between multiple conformations.