User:Megan Fleshman/Sandbox1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 8: Line 8:
The catalytic site is accessed through three different tunnels that lead from the center catalytic domain of the monomer, to the [[http://en.wikipedia.org/wiki/Lumen_(anatomy) lumen]], cytosol, and transmembrane space. The tunnels allow the entrance of reactants into the acyl transferase mechanism and the exit of the products to the correct location depending on their function.
The catalytic site is accessed through three different tunnels that lead from the center catalytic domain of the monomer, to the [[http://en.wikipedia.org/wiki/Lumen_(anatomy) lumen]], cytosol, and transmembrane space. The tunnels allow the entrance of reactants into the acyl transferase mechanism and the exit of the products to the correct location depending on their function.
The <scene name='87/877605/C_tunnel/1'>C tunnel</scene> is open to the cytosolic side of the protein in which the Acyl CoA enters into the catalytic domain.
The <scene name='87/877605/C_tunnel/1'>C tunnel</scene> is open to the cytosolic side of the protein in which the Acyl CoA enters into the catalytic domain.
 +
 +
The catalytic site contains conserved <scene name='87/877605/Catalytic_residues/1'>residues</scene> that are essential to the mechanism of the ACAT1 mechanism. These residues include His460 to function as a base catalyst and Asn421 which functions as transition state stabilization with hydrogen bonding.
 +
The <scene name='87/877605/T_tunnel/1'>T tunnel</scene> is the transmembrane tunnel in which the cholesterol enters into the catalytic domain space. Important <scene name='87/877605/T_tunnel_residues/1'>residues</scene> of the T tunnel include Arginine262, Phenylalanine 263, and Leucine 306. These residues are important for the proper entrance and orientation of the cholesterol to allow for its deprotonation in the mechanism.
The <scene name='87/877605/T_tunnel/1'>T tunnel</scene> is the transmembrane tunnel in which the cholesterol enters into the catalytic domain space. Important <scene name='87/877605/T_tunnel_residues/1'>residues</scene> of the T tunnel include Arginine262, Phenylalanine 263, and Leucine 306. These residues are important for the proper entrance and orientation of the cholesterol to allow for its deprotonation in the mechanism.
The <scene name='87/877605/L_tunnel/1'>L tunnel</scene> is used for the cholesterol ester product to be able to leave the lumen of the cell yet this exit mechanism is still unknown in addition to the cholesterol leaving to the transmembrane space through the T tunnel.
The <scene name='87/877605/L_tunnel/1'>L tunnel</scene> is used for the cholesterol ester product to be able to leave the lumen of the cell yet this exit mechanism is still unknown in addition to the cholesterol leaving to the transmembrane space through the T tunnel.
Line 25: Line 28:
== Structural highlights ==
== Structural highlights ==
-
<scene name='87/877605/Catalytic_residues/1'>Catalytic residues</scene>
+
<scene name='87/877605/Catalytic_residues/1'>residues</scene>
<scene name='87/877604/Colored_dimer/1'>Dimer of dimers</scene>
<scene name='87/877604/Colored_dimer/1'>Dimer of dimers</scene>
<scene name='87/877605/Colored_dimer_label_helices/1'>Numbered helices</scene>
<scene name='87/877605/Colored_dimer_label_helices/1'>Numbered helices</scene>

Revision as of 21:44, 5 April 2021

ACAT

Drag the structure with the mouse to rotate

References

  1. ↑ Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation. FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306 doi:http://dx.doi.org/10.1002/1873-3468.12677
  2. ↑ Qian H, Zhao X, Yan R, Yao X, Gao S, Sun X, Du X, Yang H, Wong CCL, Yan N. Structural basis for catalysis and substrate specificity of human ACAT1. Nature. 2020 May;581(7808):333-338. doi: 10.1038/s41586-020-2290-0. Epub 2020 May, 13. PMID:32433614 doi:http://dx.doi.org/10.1038/s41586-020-2290-0
  3. ↑ Guan C, Niu Y, Chen SC, Kang Y, Wu JX, Nishi K, Chang CCY, Chang TY, Luo T, Chen L. Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor. Nat Commun. 2020 May 18;11(1):2478. doi: 10.1038/s41467-020-16288-4. PMID:32424158 doi:http://dx.doi.org/10.1038/s41467-020-16288-4

Student Contributors

  • Megan Fleshman

Proteopedia Page Contributors and Editors (what is this?)

Megan Fleshman

Retrieved from "http://52.214.119.220/wiki/index.php/User:Megan_Fleshman/Sandbox1"
Personal tools