Figure 1.
Figure 1: Structure of pOC. a, Protein sequence with the
secondary structure elements indicated and the conserved
residues highlighted (green, red, blue, yellow, orange and grey
indicate conserved, acidic, basic, cysteine, asparagine and
glycine residues, respectively). Positions are identified as
conserved if more than 85% of the residues are identical, or
similar if hydrophobic in nature (see Supplementary Information
for the full sequence alignment). ' '
indicates a Gla residue, open triangles and circles indicate
hydrophobic core and Ca^2+-coordinating surface, respectively.
b, Ribbon representation of the crystal structure. The N and C
termini are labelled. Side chains of the Ca^2+-coordinating
residues and those involved in tertiary structure stabilization
are shown in stick representation. Broken grey line indicates a
hydrogen bond. c, d, Molecular surface representations of pOC
with the surface hydrophobic patch (green) and the
Ca^2+-coordinating surface (red) highlighted. Views in b and c
are perpendicular to that in d. e, Crystallographic dimer
interface. Orange and blue distinguish the two molecules. Purple
spheres and the yellow broken lines represent Ca^2+ ions and
ionic bonds, respectively.
'
indicates a Gla residue, open triangles and circles indicate
hydrophobic core and Ca^2+-coordinating surface, respectively.
b, Ribbon representation of the crystal structure. The N and C
termini are labelled. Side chains of the Ca^2+-coordinating
residues and those involved in tertiary structure stabilization
are shown in stick representation. Broken grey line indicates a
hydrogen bond. c, d, Molecular surface representations of pOC
with the surface hydrophobic patch (green) and the
Ca^2+-coordinating surface (red) highlighted. Views in b and c
are perpendicular to that in d. e, Crystallographic dimer
interface. Orange and blue distinguish the two molecules. Purple
spheres and the yellow broken lines represent Ca^2+ ions and
ionic bonds, respectively.