SOLUTION SCATTERING STUDIES OF CONFORMATIONS OF METHIONINE SYNTHASE

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. We propose to use SAXS to determine the relative arrangements of the methionine synthase domains in solution. The first experiments would examine domain arrangements in the N- and Cterminal halves of the molecule, respectively. These appear to be tractable experiments and all of the proteins are available. Longer-term aims are to examine the distribution of domains in the three-module catalytic units of MetHs from E. coli and T. maritima, and to study the ligand- and temperature-dependence of the ensemble equilibria.