|
Figure 2.
Figure 2. Individual domains of the receptor-binding protein
from phage p2. (a) The shoulder domain, with a rainbow color
gradient from the N-terminus (blue) to the C-terminus (red).
 -strands
are numbered sequentially 1-8. Dashed line indicates the absence
of residues 10-18 in the electron density map. (b) The neck -prism
domain formed by the interlaced assembly of three segments
within positions 142-163. The three faces of the -prism
are identified by the letters A, B and C; the strands in each
subunit are numbered 1-4. (c) The head domain with a rainbow
color gradient from the N-terminus (blue) to the C-terminus
(red). -strands
are numbered sequentially 1-7. The view is rotated 90° from that
in b. (d) Common double Greek-key topology shared by phage p2,
adenovirus and reovirus RBPs. The fourth strand of the Greek-key
motif is disordered in phage p2. (e) Sequence alignment of the
RBPs from phages p2, sk1 and bIL170. The secondary structure of
phage p2 RBP is indicated above the alignments and -strands
are colored red, green or blue to denote their location in the
shoulders, neck or head, respectively (alignment made by
MULTALIN
(http://prodes.toulouse.inra.fr/multalin/multalin.html)).
|
