1PKY

PYRUVATE KINASE FROM E. COLI IN THE T-STATE

Summary for 1PKY

Entry DOI	10.2210/pdb1pky/pdb
Descriptor	PYRUVATE KINASE (2 entities in total)
Functional Keywords	allostery, phosphotransferase
Biological source	Escherichia coli
Total number of polymer chains	4
Total formula weight	203181.56
Authors	Mattevi, A. (deposition date: 1995-04-27, release date: 1995-12-07, Last modification date: 2024-02-14)
Primary citation	Mattevi, A.,Valentini, G.,Rizzi, M.,Speranza, M.L.,Bolognesi, M.,Coda, A. Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition. Structure, 3:729-741, 1995 Cited by PubMed Abstract: Pyruvate kinase (PK) plays a major role in the regulation of glycolysis. Its catalytic activity is controlled by the substrate phosphoenolpyruvate and by one or more allosteric effectors. The crystal structures of the non-allosteric PKs from cat and rabbit muscle are known. We have determined the three-dimensional structure of the allosteric type I PK from Escherichia coli, in order to study the mechanism of allosteric regulation. PubMed: 8591049 DOI: 10.1016/S0969-2126(01)00207-6 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.5 Å)

Structure validation