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Papers In Press, published online ahead of print February 1, 2002
Department of Stractural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105
Corresponding Author: Jie.Zheng{at}stjude.org
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 carboxy 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 inter-helical hydrophobic interactions similar to the structures of other bacterial ACPs. The unique carboxy-terminal extension from helix IV has a "molten down" feature, and the end of the molecule being a random coil. A comparison of apo and holo forms of AcpM revealed that the 4¢-phosphopantetheine group oscillates between two states, one is bound to a hydrophobic groove on the surface of AcpM, and another 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 carboxy 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.
J. Biol. Chem, 10.1074/jbc.M112300200
Submitted on December 21, 2001
Revised on February 1, 2002
Accepted on February 1, 2002
The solution structure of acyl carrier protein from mycobacterium tuberculosis
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