1QD1

THE CRYSTAL STRUCTURE OF THE FORMIMINOTRANSFERASE DOMAIN OF FORMIMINOTRANSFERASE-CYCLODEAMINASE.

Summary for 1QD1

• Entry DOI: 10.2210/pdb1qd1/pdb
• Descriptor: FORMIMINOTRANSFERASE-CYCLODEAMINASE, N-{[4-({[(6R)-2-amino-5-formyl-4-oxo-1,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)phenyl]carbonyl}-L-glutamic acid, GLYCEROL, ... (4 entities in total)
• Functional Keywords: functional dimer, alpha-beta-beta-alpha sandwich, electrostatically charged substrate tunnel, transferase
• Biological source: Sus scrofa (pig)
• Cellular location: Cytoplasm, cytoskeleton, centrosome, centriole (By similarity): P53603
• Total number of polymer chains: 2
• Total formula weight: 72888.89

Authors

Kohls, D.,Sulea, T.,Purisima, E.,MacKenzie, R.E.,Vrielink, A. (deposition date: 1999-07-08, release date: 2000-01-12, Last modification date: 2024-02-14)

Primary citation

Kohls, D.,Sulea, T.,Purisima, E.O.,MacKenzie, R.E.,Vrielink, A.
The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme.
Structure Fold.Des., 8:35-46, 2000

PubMed Abstract: The bifunctional enzyme formiminotransferase-cyclodeaminase (FTCD) contains two active sites at different positions on the protein structure. The enzyme binds a gamma-linked polyglutamylated form of the tetrahydrofolate substrate and channels the product of the transferase reaction from the transferase active site to the cyclodeaminase active site. Structural studies of this bifunctional enzyme and its monofunctional domains will provide insight into the mechanism of substrate channeling and the two catalytic reactions.

PubMed: 10673422
DOI: 10.1016/S0969-2126(00)00078-2

Experimental method

X-RAY DIFFRACTION (1.7 Å)