User:James Bahng/sandbox 1
From Proteopedia
(Difference between revisions)
| Line 18: | Line 18: | ||
== Structural highlights == | == Structural highlights == | ||
| - | FAH is a homodimer made up of two 46 kDa subunits.<ref name=”placeholder”> | + | FAH is a homodimer made up of two 46 kDa subunits.<ref name=”placeholder”> Bateman, R.L., Bhanumoorthy, P., Witte, J.F., McClard, R.W., Grompe, M., Timm, D.E. (2001) Mechanistic Inferences from the Crystal Structure of Fumarylacetoacetate Hydrolase with a Bound |
| + | Phosphorus-based Inhibitor. Journal of Biological Chemistry, 207(18) 15284-15291 | ||
| + | </ref> The subunits form a cavity <scene name='58/581360/Close_up_showing_metal_ions/2'>complementary in shape and charge to fumarylacetoacetate</scene>. The binding is coordinated by Ca2+, Arg and two Tyr(INSERT IMAGE LINK). The active residues in are His-133, acting as a base to activate a water, and Arg-237, Gln-240 and Lys-253 (INSERT IMAGE LINK)acting to stabilize the tetrahedral alkoxy transition state. | ||
| - | |||
| - | 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. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
| - | + | <references/> | |
| - | + | ||
Revision as of 04:43, 1 April 2014
Structure of Fumarylacetoacetate Hydrolase with Phosphorus-based Inhibitor
| |||||||||||
References
- ↑ Bateman, R.L., Bhanumoorthy, P., Witte, J.F., McClard, R.W., Grompe, M., Timm, D.E. (2001) Mechanistic Inferences from the Crystal Structure of Fumarylacetoacetate Hydrolase with a Bound Phosphorus-based Inhibitor. Journal of Biological Chemistry, 207(18) 15284-15291
