1klp
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1klp.jpg|left|200px]] | [[Image:1klp.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1klp", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1klp| PDB=1klp | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''The Solution Structure of Acyl Carrier Protein from Mycobacterium tuberculosis''' | '''The Solution Structure of Acyl Carrier Protein from Mycobacterium tuberculosis''' | ||
| Line 30: | Line 27: | ||
[[Category: Zhang, Y M.]] | [[Category: Zhang, Y M.]] | ||
[[Category: Zheng, J.]] | [[Category: Zheng, J.]] | ||
| - | [[Category: | + | [[Category: Four-helix bundle]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:53:31 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:53, 2 May 2008
The Solution Structure of Acyl Carrier Protein from Mycobacterium tuberculosis
Overview
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.
About this Structure
1KLP is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
The solution structure of acyl carrier protein from Mycobacterium tuberculosis., Wong HC, Liu G, Zhang YM, Rock CO, Zheng J, J Biol Chem. 2002 May 3;277(18):15874-80. Epub 2002 Feb 1. PMID:11825906 Page seeded by OCA on Fri May 2 22:53:31 2008
