PMID:14995075
| Citation |
Orun, O, Koch, MH, Kan, B, Svergun, DI, Petoukhov, MV and Sayers, Z (2003) Structural characterization of T-protein of the Escherichia coli glycine cleavage system by X-ray small angle scattering. Cell. Mol. Biol. (Noisy-le-grand) 49 Online Pub:OL453-9 |
|---|---|
| Abstract |
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. |
| Links | |
| Keywords |
Aminomethyltransferase; Chromatography; Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/isolation & purification; Hydroxymethyl and Formyl Transferases/chemistry; Hydroxymethyl and Formyl Transferases/isolation & purification; Models, Molecular; Protein Structure, Tertiary; Scattering, Radiation; X-Rays |
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