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Originally published In Press as doi:10.1074/jbc.M112300200 on February 1, 2002

J. Biol. Chem., Vol. 277, Issue 18, 15874-15880, May 3, 2002
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The Solution Structure of Acyl Carrier Protein from Mycobacterium tuberculosis*

Hing C. WongDagger §, Gaohua LiuDagger §, Yong-Mei Zhang§, Charles O. Rock||, and Jie ZhengDagger ||**

From the Departments of Dagger  Structural Biology and  Infectious Diseases, St. Jude Children's Research Hospital, Memphis, Tennessee 38105 and the || Department of Molecular Sciences, University of Tennessee, Memphis, Tennessee 38163

Acyl carrier protein (ACP) performs the essential function of shuttling the intermediates between the enzymes that constitute the type II fatty acid synthase system. Mycobacterium tuberculosis is unique in producing extremely long mycolic acids, and tubercular ACP, AcpM, is also unique in possessing a longer carboxyl terminus than other ACPs. We determined the solution structure of AcpM using protein NMR spectroscopy to define the similarities and differences between AcpM and the typical structures. The amino-terminal region of the structure is well defined and consists of four helices arranged in a right-handed bundle held together by interhelical hydrophobic interactions similar to the structures of other bacterial ACPs. The unique carboxyl-terminal extension from helix IV has a "melted down" feature, and the end of the molecule is a random coil. A comparison of the apo- and holo-forms of AcpM revealed that the 4'-phosphopantetheine group oscillates between two states; in one it is bound to a hydrophobic groove on the surface of AcpM, and in another it is solvent-exposed. The similarity between AcpM and other ACPs reveals the conserved structural motif that is recognized by all type II enzymes. However, the function of the coil domain extending from helix IV to the carboxyl terminus remains enigmatic, but its structural characteristics suggest that it may interact with the very long chain intermediates in mycolic acid biosynthesis or control specific protein-protein interactions.

* This work was supported by National Institutes of Health Grants GM34496, AI49320, and GM61739, Cancer Center (CORE) Support Grant CA 21765, and the American Lebanese Syrian Associated Charities. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates of the final 20 structures (code 1KLP) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/) and the BioMagResBank.

§ These authors contributed equally to this work.

** To whom correspondence should be addressed: Dept. of Structural Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, Memphis, TN 38105. Tel.: 901-495-3168; Fax: 901-495-3032; E-mail: jie.zheng@stjude.org.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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