Structural characterization of T-protein of the Escherichia coli glycine cleavage system by X-ray small angle scattering.
T-protein, one of the components of the glycine cleavage complex, catalyses the formation of ammonia and methylene-tetrahydrofolate from H-protein-bound intermediate. Native T-protein of the glycine cleavage system from E. coli was efficiently purified using a combination of hydrophobic interaction, gel permeation and ion exchange chromatography. Synchrotron radiation small angle X-ray solution scattering indicates that T-protein has an extended structure in solution. A low resolution model of the protein was constructed ab initio and tentative models of the tertiary structure were built using prediction methods constrained by the scattering data.
Orun
O
O
Department of Biophysics, Marmara University, School of Medicine, 34716, Istanbul, Turkey. oyaorun@yahoo.com
Koch
M H J
MH
Kan
B
B
Svergun
D I
DI
Petoukhov
M V
MV
Sayers
Z
Z
D050960:Aminomethyltransferase; D002845:Chromatography; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000302:isolation & purification; D019877:Hydroxymethyl and Formyl Transferases / Q000737:chemistry* / Q000302:isolation & purification; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D012542:Scattering, Radiation; D014965:X-Rays
D029968:Escherichia coli Proteins; D019877:Hydroxymethyl and Formyl Transferases; D050960:Aminomethyltransferase