Article
Swiveling domain mechanism in pyruvate phosphate dikinase.
Biochemistry - 25 Dec 2007
Lim Kap, Read Randy J, Chen Celia C H, Tempczyk Aleksandra, Wei Min, Ye Dongmei, Wu Chun, Dunaway-Mariano Debra, Herzberg Osnat
Abstract excerpt
Pyruvate phosphate dikinase (PPDK) catalyzes the reversible conversion of phosphoenolpyruvate (PEP), AMP, and Pi to pyruvate and ATP. The enzyme contains two remotely located reaction centers: the nucleotide partial reaction takes place at the N-terminal domain, and the PEP/pyruvate partial reaction takes place at the C-terminal domain. A central domain, tethered to the N- and C-terminal domains by two closely...
Topics
- Binding Sites
- Clostridium symbiosum
- Crystallography, X-Ray
- Isoenzymes
- Kinetics
- Mutation
- Nucleotides
- Protein Structure, Quaternary
- Protein Structure, Tertiary
- Pyruvate, Orthophosphate Dikinase
- Structural Homology, Protein