Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochem Biophys Res Commun. 2006 Mar 17;341(3):776-83. Epub 2006 Jan 19.

NMR studies of Escherichia coli acyl carrier protein: dynamic and structural differences of the apo- and holo-forms.

Author information

1
Department of Chemistry and Bio/Molecular Informatics Center, Konkuk University, 1 Hwayang-dong, Kwangjin-gu, Seoul 143-701, Republic of Korea. ymkim@konkuk.ac.kr

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.

PMID:
16455053
DOI:
10.1016/j.bbrc.2006.01.025
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center