Structural and Biophysical Characterization of Rab5a from Leishmania donovani

Leishmania donovani possess two isoforms of Rab5, Rab5a and Rab5b, which are involved in fluid phase and receptor mediated endocytosis, respectively. We have characterized the solution structure and dynamics of a stabilized truncated LdRab5a mutant. For the purpose of NMR structure determination, protein stability was enhanced by systematically introducing various deletions and mutations. Deletion of hypervariable C-terminal and the 20 residues LdRab5a specific insert slightly enhanced the stability, which was further improved by C107S mutation.

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