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Figure 5.
Figure 5 Surface features of InlB GW domains. (A) Top: ribbon
representation of the three InlB GW domains. The first GW domain
is proteolytically sensitive and cleaved from the second and
third protease-resistant GW domains at Leu464. Middle:
electrostatic surface potential of the GW domains (red = -10 kT,
blue = +10 kT). Bottom: exposed hydrophobic residues (green)
mapped to the molecular surface of the GW domains. The black
arrow indicates the hydrophobic groove between domains 1 and 2.
(B) Basis for GW[A]–GW[B] pairwise association. Top: ribbon
representations of GW[A] domains (left) and GW[B] domains
(right). Bottom: molecular surface representation (green,
hydrophobic; red, acidic; blue, basic), with GW[A] and GW[B]
rotated to show interface residues (numbered).
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