|
|
| (8 intermediate revisions by 3 users not shown) |
| Line 1: |
Line 1: |
| {{Sandbox_Reserved_Butler_CH462_Sp2015_#}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | | {{Sandbox_Reserved_Butler_CH462_Sp2015_#}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->*[[User:Isaac C. Gluesenkamp/Sandbox 1]] |
| | ==Your Protein Name here== |
| | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>Zinc Dependent MarR Family Transcriptional Regulator AdcR |
| | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. |
| | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. |
|
| |
|
| | == Biological Function == |
|
| |
|
| ==Your Heading Here (maybe something like 'Structure')== | | == Structural Overview == |
|
| |
|
| <StructureSection load='3r44' size='340' side='right' caption='Very Long Chain Fatty Acyl CoA Synthetase (FadD13)' scene='69/694232/Opening_scene/1'>
| | == Mechanism of Action == |
|
| |
|
| == General mechanism for the activation of fatty acids == | | == Zinc Ligand(s) == |
| 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).
| |
|
| |
|
| =active site (to be copied over)= | | == Other Ligands == |
| | |
| A high conserved residue in the C-terminal region, <scene name='69/694233/Lys_487/2'>Lysine 487</scene>, resulted in a 95% loss of function of FadD13 and is thought to be involved in the orientation of the substrates to form the adenylate intermediate.<ref name="residue paper">PMID: 20027301</ref> Other mutation studies, found that Serine 404 was involved in the binding of Coenzyme A which may only occur once the region incurs a 140 degree rotational change.<ref name="Our Paper"/><ref name="residue paper"/>
| |
| | |
| | |
| | |
| | |
| == Function ==
| |
| | |
| | |
| This is the <scene name='69/694232/Arginine_rich_lid_loop/1'>Arginie-rich lid loop</scene>.<ref name="OUR PAPER">PMID: 22560731</ref>
| |
| | |
| This is the <scene name='69/694232/Linker_section/2'>linker</scene>.<ref name="OUR PAPER"/>
| |
| | |
| FadD13 has three different <scene name='69/694232/Domains/2'>regions</scene>: 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 <scene name='69/694232/Adenine_binding_group/2'>six amino acids (300-305)</scene> that is structurally identically to other acyl-CoA synthetases (Citation for original paper).
| |
| | |
| citation 1 <ref name="Our Paper">PMID: 22560731</ref>
| |
| <ref name="OUR PAPER"/>
| |
| | |
| citation 2 <ref name="JT">PMID: 20454815</ref>
| |
| <ref name="JT"/>
| |
| | |
| Citation 3 <ref name="SM">PMID: 12164478</ref>
| |
| <ref name="SM"/>
| |
| | |
| | |
| == Disease ==
| |
| | |
| == Relevance ==
| |
| | |
| == Structural highlights ==
| |
|
| |
|
| This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. |
