Sandbox Reserved 653: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 15: | Line 15: | ||
'''Structure:''' | '''Structure:''' | ||
The structure of Aspartate Aminotransferase has been determined through studies using X-ray crystallography. It is seen that AST has two identical subunits. Each subunit is approximately 300 residues long and each is composed of both a small and large domain. In addition a third domain is present which consists of the N-terminal residues 3-14; these residues link and stabilize the two subunits by forming a strand. Pyridoxial phosphate (PLP), the cofactor for AST binds to the large domain, interacting with the amino group of the Lys258 residue. It also interacts through hydrogen bonding with the Asp222 and Tyr 225 residues within the large domain. The small domain is responsible for the shift of the enzyme from an open conformation to closed conformation. This shift is based on the binding of the substrate. | |||
<scene name='Sandbox_Reserved_653/Active_sites/1'>active sites </scene> | <scene name='Sandbox_Reserved_653/Active_sites/1'>active sites </scene> | ||
