Structural highlights
Function
CISY_PIG
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of pig heart citrate synthase at 1.78 A resolution.,Larson SB, Day JS, Nguyen C, Cudney R, McPherson A Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt, 5):430-4. Epub 2009 Apr 24. PMID:19407370[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Larson SB, Day JS, Nguyen C, Cudney R, McPherson A. Structure of pig heart citrate synthase at 1.78 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt, 5):430-4. Epub 2009 Apr 24. PMID:19407370 doi:10.1107/S1744309109008343
