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A diacylated 15 kDa protein named SMP-1 (Small Myrisotylated Protein-1) which is targeted to the flagellar membrane of Leishmania species has been characterized (Tull et al., 2004). SMP-1 belongs to a new family of Leishmania proteins which are relatively well conserved except for differences in their C-terminal regions and in their N-terminal acylation patterns. These proteins have not been functionally characterized, but differ in their membrane targeting and therefore we are determining the structures of these proteins. SMP-1 (residues 1–131) was overexpressed and 15N or 13C/15N labelled. Assignment of backbone and sidechain resonances was straightforward using a combination of triple resonance experiments. Backbone assignments were complete except for the Ha of Met-1 and Ser-6, and HN of Ser-7 and-111. Assignment of side chain resonances is near complete (95% of non-exchangeable 1H …