Figure 3.

Sequence alignment of XOL-1. (A) Structure-based sequence alignment of XOL-1 within GHMP kinase conserved motif regions. Sequence of XOL-1 (bottom) is aligned with structurally equivalent residues from other GHMP kinases. The three GHMP conserved motifs are highlighted in yellow. In XOL-1, these residues are as follows: motif1, residues P45-S53; motif2, residues D120-P128; and motif3, V298-G302. Tandem serines of motif2 are highlighted by boxes. The sequence of XOL-1 is highly divergent, even within conserved motifs, from other GHMP kinases with only one structurally equivalent residue found to be identical (Gly 123 in motif2) throughout the entire sequence. Residues conserved identically in all structures are in red. Highly conserved residues are in blue. Secondary structure is assigned above. PMK, phosphomevalonate kinase; MVK_mj, mevalonate kinase (M. jannaschii); MVK_rn, mevalonate kinase (R. norvegicus); MVPD, mevalonate-5-phosphate decarboxylase; HSK, homoserine kinase; XOL_c, XOL-1 (C. briggsae); XOL_ce, XOL-1 (C. elegans). (B) Alignment of C. elegans and C. briggsae XOL-1 sequences. The C. elegans and C. briggsae XOL-1 sequences were aligned by the clustal method (GONNET series). Gaps and insertions incompatible with the structure were edited manually. Residues corresponding to GHMP conserved motifs are highlighted in yellow. A conserved acidic C-terminal motif is highlighted in green. Identically conserved residues are highlighted in red and conservatively substituted residues are in blue. Secondary structure is assigned above.