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Figure 1


Fig. 1. Sequence similarity between the mammalian major vault protein (MVP) and the bacterial tellurite resistance protein (TelA). (A) Schematic diagram of the major vault protein (MVP). Human MVP is composed of an amino-terminal domain (aa 26–401) comprising a series of seven imperfect repeats (blue circles) and a carboxyl-terminal region (black bar) that contains a coiled-coil domain (aa 652–800). (B) Sequence alignment of the repeat unit of MVP with TelA. Residue number corresponds to the consensus gapped sequence and thus does not correspond perfectly to that of either constituent sequence. Amino acid symbols are colored according to quality of match, with red indicating perfect conservation (redundantly labeled with a asterisk in the bottom line), green indicating substantial similarity (colon, strong similarity; stop, moderate similarity) and light blue indicating a mismatch. The line labeled `Prim. Cons.' reports known residues within the consensus sequence (dark blue script). The portion of the MVP sequence structurally resolved in NMR studies (Kozlov et al., 2005) is underlined with a bar colored according to observed secondary structure: magenta for helices, yellow for beta strands, and black for coils and turns.





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