THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION

RESIDUE 246 OF EACH ALPHA SUBUNIT IS A PHOSPHORYLATED HISTIDINE.

The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution.

Crystallization of Succinyl-Coa Synthetase from Escherichia Coli

AMINO-TERMINAL ANALYSIS OF THE ALPHA SUBUNIT INDICATES THAT THE FIRST RESIDUE IS A SERINE (W. A. BRIDGE, ENZYMES, 3RD ED. 10, 581-606 (1974)). IN THE GENE SEQUENCING PAPER, BUCK, SPENCER AND GUEST STATE THAT "[THE ASSUMPTION IS] THAT THE INITIATING FORMYLMETHIONINE IS REMOVED POSTTRANSLATIONALLY FROM THE ALPHA BUT NOT FROM THE BETA SUBUNIT" (D. BUCK, M. E. SPENCER, AND J. R. GUEST, BIOCHEMISTRY 24, 6245-6252 (1985)).

SUCCINYL-COA SYNTHETASE (SUCCINATE-COA LIGASE) (ADP-FORMING) (E.C.6.2.1.5)