Structure of pig heart citrate synthase at 1.78 A resolution.
Pig heart citrate synthase was crystallized from a small-molecule cocktail containing cystamine dihydrochloride, aspartame and benzamidine hydrochloride. The structure was refined to an R factor of 0.179 (R(free) = 0.222) using synchrotron data to a resolution of 1.78 A. The model includes the full-length protein, a chloride ion, a sulfate ion, 305 water molecules and an unexpected moiety attached through a disulfide linkage to Cys184, which was modeled as a half-cystamine molecule generated by disulfide exchange with the cystamine in the small-molecule cocktail.
Larson
Steven B
SB
Department of Molecular Biology and Biochemistry, The University of California, Irvine, 92697-3900, USA.
Day
John S
JS
Nguyen
Chieugiang
C
Cudney
Robert
R
McPherson
Alexander
A
D000818:Animals; D002950:Citrate (si)-Synthase / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D009206:Myocardium / Q000201:enzymology*; D017434:Protein Structure, Tertiary; D034421:Sus scrofa / Q000235:genetics
D002950:Citrate (si)-Synthase