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J. Biol. Chem., Vol. 276, Issue 11, 8231-8238, March 16, 2001
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From the Departments of The molecular details that govern the specific
interactions between acyl carrier protein (ACP) and the enzymes of
fatty acid biosynthesis are unknown. We investigated the mechanism of
ACP·protein interactions using a computational analysis to
dock the NMR structure of ACP with the crystal structure of
The atomic coordinates and the structure factors (code 1G5|ga) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
Identification and Analysis of the Acyl Carrier Protein (ACP)
Docking Site on
-Ketoacyl-ACP Synthase III*
,,
,**, and**
Biochemistry and
Structural Biology, St. Jude Children's Research Hospital,
Memphis, Tennessee 38105, the § Department of Molecular
Biology, The Scripps Research Institute, La Jolla, California 92037, and the ** Department of Biochemistry, University of Tennessee, Memphis,
Tennessee 38163
-ketoacyl-ACP synthase III (FabH) and experimentally tested the
model by the biochemical analysis of FabH mutants. The activities of
the mutants were assessed using both an ACP-dependent and
an ACP-independent assay. The ACP interaction surface was defined by
mutations that compromised FabH activity in the
ACP-dependent assay but had no effect in the
ACP-independent assay. ACP docked to a positively charged/hydrophobic patch adjacent to the active site tunnel on FabH, which included a
conserved arginine (Arg-249) that was required for ACP docking. Kinetic analysis and direct binding studies between FabH and ACP confirmed the identification of Arg-249 as critical for FabH·ACP interaction. Our experiments reveal the significance of the positively charged/hydrophobic patch located adjacent to the active site cavities
of the fatty acid biosynthesis enzymes and the high degree of sequence
conservation in helix II of ACP across species.
*
This work was supported by National Institutes of Health
Grants GM34496 (to C. O. R.), GM44973 (to S. W. W.), and Cancer
Center (CORE) Support Grant CA 21765 and by the American Lebanese
Syrian Associated Charities.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Biochemistry, St. Jude Children's Research Hospital, Memphis, TN
38105. Tel.: 901-495-3491; Fax: 901-525-8025; E-mail:
charles.rock@stjude.org.
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