2r82
From Proteopedia
Contents |
Pyruvate phosphate dikinase (PPDK) triple mutant R219E/E271R/S262D adapts a second conformational state
Template:ABSTRACT PUBMED 18052212
About this Structure
2r82 is a 1 chain structure with sequence from Clostridium symbiosum. Full crystallographic information is available from OCA.
See Also
Reference
- Lim K, Read RJ, Chen CC, Tempczyk A, Wei M, Ye D, Wu C, Dunaway-Mariano D, Herzberg O. Swiveling domain mechanism in pyruvate phosphate dikinase. Biochemistry. 2007 Dec 25;46(51):14845-53. Epub 2007 Dec 4. PMID:18052212 doi:http://dx.doi.org/10.1021/bi701848w
- Herzberg O, Chen CC, Liu S, Tempczyk A, Howard A, Wei M, Ye D, Dunaway-Mariano D. Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis. Biochemistry. 2002 Jan 22;41(3):780-7. PMID:11790099
- McGuire M, Huang K, Kapadia G, Herzberg O, Dunaway-Mariano D. Location of the phosphate binding site within Clostridium symbiosum pyruvate phosphate dikinase. Biochemistry. 1998 Sep 29;37(39):13463-74. PMID:9753432 doi:http://dx.doi.org/10.1021/bi980920i
- Wei M, Li Z, Ye D, Herzberg O, Dunaway-Mariano D. Identification of domain-domain docking sites within Clostridium symbiosum pyruvate phosphate dikinase by amino acid replacement. J Biol Chem. 2000 Dec 29;275(52):41156-65. PMID:10995759 doi:http://dx.doi.org/10.1074/jbc.M006149200
Categories: Clostridium symbiosum | Pyruvate, phosphate dikinase | Chen, C C. | Herzberg, O. | Lim, K. | Read, R J. | Atp-binding | Conformational transition | Kinase | Magnesium | Metal-binding | Nucleotide-binding | Phosphorylation | Phosphotransferase | Remote active site | Swiveling domain | Transferase