1KLP

The Solution Structure of Acyl Carrier Protein from Mycobacterium tuberculosis

Summary for 1KLP

• Entry DOI: 10.2210/pdb1klp/pdb
• Descriptor: MEROMYCOLATE EXTENSION ACYL CARRIER PROTEIN (1 entity in total)
• Functional Keywords: four-helix bundle, ligand transport
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cytoplasm (By similarity): P0A4W6
• Total number of polymer chains: 1
• Total formula weight: 12532.87

Authors

Wong, H.C.,Liu, G.,Zhang, Y.-M.,Rock, C.O.,Zheng, J. (deposition date: 2001-12-12, release date: 2002-06-07, Last modification date: 2024-05-01)

Primary citation

Wong, H.C.,Liu, G.,Zhang, Y.M.,Rock, C.O.,Zheng, J.
The solution structure of acyl carrier protein from Mycobacterium tuberculosis.
J.Biol.Chem., 277:15874-15880, 2002

PubMed Abstract: 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.

PubMed: 11825906
DOI: 10.1074/jbc.M112300200

Experimental method

SOLUTION NMR