Sandbox Reserved 1065

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This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. Click the 3D button (when editing, above the wikitext box) to insert Jmol. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

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spinqualitylabelsall models Very Long Chain Fatty Acyl CoA Synthetase (FadD13) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 General mechanism for the activation of fatty acids 2 Function 3 Disease 4 Relevance 5 Structural highlights General mechanism for the activation of fatty acids FadD13 first activates the fatty acid through a reaction with ATP to form an acyl adenylate intermediate and release pyrophosphate. Following a conformational change of the enzyme, coenzyme A is able to bind and reaction with the acyl adenylate intermediate forming the acyl CoA product (Figure 1). Function This is the .[1] This is the .[1] FadD13 has three different : The N-terminal region (1-395) is in blue, the C-terminal region (402-403) is in red, and the six amino acid linker is in tan (citation for original paper). The adenine of ATP is bound to a group of that is structurally identically to other acyl-CoA synthetases (Citation for original paper). citation 1 [2] [1] citation 2 [3] [3] Citation 3 [4] [4] Disease Relevance Structural highlights This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

1. ↑ ^{1.0 1.1 1.2} Andersson CS, Lundgren CA, Magnusdottir A, Ge C, Wieslander A, Molina DM, Hogbom M. The Mycobacterium tuberculosis Very-Long-Chain Fatty Acyl-CoA Synthetase: Structural Basis for Housing Lipid Substrates Longer than the Enzyme. Structure. 2012 May 2. PMID:22560731 doi:10.1016/j.str.2012.03.012
2. ↑ Andersson CS, Lundgren CA, Magnusdottir A, Ge C, Wieslander A, Molina DM, Hogbom M. The Mycobacterium tuberculosis Very-Long-Chain Fatty Acyl-CoA Synthetase: Structural Basis for Housing Lipid Substrates Longer than the Enzyme. Structure. 2012 May 2. PMID:22560731 doi:10.1016/j.str.2012.03.012
3. ↑ ^{3.0 3.1} Jatana N, Jangid S, Khare G, Tyagi AK, Latha N. Molecular modeling studies of Fatty acyl-CoA synthetase (FadD13) from Mycobacterium tuberculosis--a potential target for the development of antitubercular drugs. J Mol Model. 2011 Feb;17(2):301-13. doi: 10.1007/s00894-010-0727-3. Epub 2010 May, 8. PMID:20454815 doi:http://dx.doi.org/10.1007/s00894-010-0727-3
4. ↑ ^{4.0 4.1} Schroeder EK, de Souza N, Santos DS, Blanchard JS, Basso LA. Drugs that inhibit mycolic acid biosynthesis in Mycobacterium tuberculosis. Curr Pharm Biotechnol. 2002 Sep;3(3):197-225. PMID:12164478