Sandbox Reserved 1063
From Proteopedia
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== References == | == 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 | + | #1 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 |
[http://www.proteopedia.org/wiki/index.php/3r44] | [http://www.proteopedia.org/wiki/index.php/3r44] | ||
Revision as of 12:56, 7 April 2015
Introduction
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. Below is the general mechanism for ACS proteins.
Image:FadD13 steps.jpg
Mechanism
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References
- 1 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
