NMR Studies of Escherichia Coli Acyl Carrier Protein: Dynamic and Structural Differences of the Apo- and Holo-forms

Authors

Yangmee Kim, Konkuk University
Evgueni Kovriguine, Marquette UniversityFollow
Ziad Eletr, University of Georgia

Document Type

Article

Publication Date

3-2006

Source Publication

Biochemical and Biophysical Research Communications

Abstract

Two indicators of conformational variability of Escherichia coli acyl carrier protein (ACP) have been investigated, namely backbone dynamics and chemical shift variations of ACP. Hydrophobic interactions between the 4′-PP prosthetic group and the hydrophobic pocket enclosed by the amphipathic helices resulted in chemical shift perturbations in the residues near the prosthetic group binding sites and contact sites in the hydrophobic pockets upon conversion from apo- to holo-forms. At pH 7.9, destabilization of ACP due to negative charge repulsions and the deprotonated state of His 75 resulted in observed chemical shift changes in the C-terminal region. Model-free analysis showed that the α₁α₂ loop region near the prosthetic group binding site in ACP shows the greatest flexibility (lowest S² values) and this result may suggest these flexibilities are required for structural rearrangements when the acyl chain binds to the prosthetic group of ACP. Flexibility of ACP shown in this study is essential for its ability to interact with functionally different enzyme partners specifically and weakly in the rapid delivery of acyl chain from one partner to another.

Comments

Accepted version. Biochemical and Biophysical Research Communications, Vol. 341, No. 3 (March 2006): 776-783. DOI: © 2006 Elsevier Inc. Used with permission.

Recommended Citation

Kim, Yangmee; Kovriguine, Evgueni; and Eletr, Ziad, "NMR Studies of Escherichia Coli Acyl Carrier Protein: Dynamic and Structural Differences of the Apo- and Holo-forms" (2006). Chemistry Faculty Research and Publications. 231.
https://epublications.marquette.edu/chem_fac/231