Cystathionine gamma-lyase (CSE) is a member of the gamma family of PLP-dependent enzymes (which bind to pyridoxal-5'-phosphate for reaction catalysis), along with other enzymes such as cystathionine gamma-synthase, Cystathionine beta-lyase, and Methionine gamma-lyase. Similar to other enzymes in this family, CSE exhibits a tetrameric structure with D2 symmetry.
Functions
Structure
Cystathionine gamma-lyase exhibits a tetrameric quaternary structure when bound to its ligand (PLP), and in its apo form, it can exist as both a monomer and a tetramer, with the latter being more predominant (2). The monomer comprises two domains: a and a smaller domain.
The larger domain is characterized by the presence of an alpha/beta/alpha structure, and a mixed beta-sheet surrounded by eight alpha-helices. On the other hand, the smaller domain possesses a four-stranded antiparallel beta-sheet and three alpha-helices on one side of the beta-sheet.
Disease
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.
