Sandbox Reserved 1063
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | There are many portions of the FadD13 enzyme the play very pivotal roles in its function. The first important structural point of note is that there are two sub units, the larger N-terminal sub unit (residues 1-395) and the smaller C-terminal sub unit (residues 402-503) held together by a six amino acid linker (<scene name='69/694230/Residues_396-401/1'>residues 396-401</scene>). <scene name='69/694230/Atp_and_amp_binding_region/1'>ATP and AMP Binding Region</scene> | + | There are many portions of the FadD13 enzyme the play very pivotal roles in its function. The first important structural point of note is that there are two sub units, the larger N-terminal sub unit (<scene name='69/694230/N-terminal_domain/1'>residues 1-395</scene>) and the smaller C-terminal sub unit (residues 402-503) held together by a six amino acid linker (<scene name='69/694230/Residues_396-401/1'>residues 396-401</scene>). <scene name='69/694230/Atp_and_amp_binding_region/1'>ATP and AMP Binding Region</scene> |
== Function == | == Function == | ||
Revision as of 13:13, 31 March 2015
Structure
in Mycobacterium Tuberculosis is an ACSVL (Acyl-CoA synthetases very long) peripheral membrane protein. ACS proteins activate lipids and fatty acids before going into metabolic pathways. FadD13 is soluble unlike other ACSVL proteins. FadD13 contains a hydrophobic tunnel for fatty acids to bind to, as well as an arginine rich lid loop that binds to the cell membrane. The binding of ATP causes structural changes promoting the binding of the hydrophobic substrates. Formation of an acyl-adenylate intermediate induces a 140 degree rotation of the small domain and binding of CoA for production of the final product, a fatty acyl-CoA thioester.
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References
Andersson, C.S., Lundgren, C.A.K., Magnusdottir, A., Ge, C., Weislander, A., Molina, D., Hogbom, M. (2012)The Mycobacterium tuberculosis Very-Long-Chain Fatty Acyl-CoA Synthetase: structural Basis for Housing Lipid Substrates longer than the Enzyme. Cell Press,1062-1070
