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.
Department of Biophysics, Marmara University, School of Medicine, 34716, Istanbul, Turkey. oyaorun@yahoo.com
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Orun
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Koch
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Kan
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Svergun
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Petoukhov
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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