These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: NMR studies of Escherichia coli acyl carrier protein: dynamic and structural differences of the apo- and holo-forms.
    Author: Kim Y, Kovrigin EL, Eletr Z.
    Journal: Biochem Biophys Res Commun; 2006 Mar 17; 341(3):776-83. PubMed ID: 16455053.
    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 alpha(1)alpha(2) loop region near the prosthetic group binding site in ACP shows the greatest flexibility (lowest S(2) 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.
    [Abstract] [Full Text] [Related] [New Search]