The anatomy of a kinase and the control of phosphate transfer

Abstract

Table of contents Basic features of phosphoglycerate kinase (PGK), The sequences and crystal structures of PGK NMR studies of the structure of the protein PGK, Thermal analysis of yeast PGK, Additional data from NMR studies Substrate binding, Nucleotide binding site: MgATP and MgADP, The function of magnesium, The triose substrate binding site, NMR analysis of substrate binding: summary, General anion‐binding site The conformation change, Kinetic studies of the reaction, Site‐specific mutagenesis studies Effects of mutations on protein structure in the absence of substrates, Mutations in the interdo‐main region, Mutations in the basic patch Effect of Gri3P binding on mutant proteins, Mutations in the interdomain region, Mutations in the basic patch Effects of mutations on kinetics of PGK, Mutations in the interdomain region, Mutations in the basic patchConclusions from experiments with mutants Kinetic effects of low sulphate concentration, Interdomain region, Basic patch region The so‐called hinge of proteins, Features of PGK Common features with other NTP‐utilising systems, The nucleotide‐binding site, The catalytic loop, Domain closure Comments on mechanical devices in multi‐protein enzymes