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Figure 4.
Fig. 4. Characterization of the putative tip-interaction
interface of a T3SS needle. (A) Surface representation of the
side view of the T3SS needle with each monomer colored
differently, starting from red and circling the needle to
purple. Residues likely to effect interactions with the tip
complex are highlighted as follows: P44 and Q51 in Shigella
(white) and the equivalent of D46 in Yersinia (gray). (B) View
and coloring as for A, with residues conserved between Shigella
MxiH and Yersinia YscF highlighted. Residues conserved in the
head domain: L37, P41, N43, P44, L46, L47, A48, and Q51 (white);
in the tail domain, N62, S65, V68, K72, D73, I78, Q80, and F82
(gray) are shown for the top circle of the needle. (C Left)
Ribbon diagram of LcrV (30) colored N (blue) to C (red) termini.
(C Right) Overlay of the C-terminal helices of MxiH (red,
residues 45–75) and LcrV (blue, residues 287–317), with all
but the overlaid region made transparent to aid visualization.
(D) Model of an LcrV tip complex (surface representation, gray)
onto the tip of a T3SS needle.
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