Fig. 4: The structural basis of chitinase incorporation into the YenTc shell. | Nature Communications

Fig. 4: The structural basis of chitinase incorporation into the YenTc shell.

From: Complete structures of the YenTc holotoxin prepore and pore reveal the evolutionary basis for chitinase incorporation into ABC toxins

Fig. 4: The structural basis of chitinase incorporation into the YenTc shell.

A Architecture of the CBDs and chitinases from YenTc (right). B Structural overview of how CBD-A (red) interfaces with the Chi2NTD (cyan) and Chi2 (grey). The interface is stabilised by interacting loops at each end of the complementary, antiparallel CBD-A β-acceptor (red) and Chi2 β-donor (blue) interface. The complementary antiparallel interface is stabilised further by a hydrophobic interaction, where the Chi2 β-donor occupies a hydrophobic cleft formed by the CBD-A β-acceptor. C The interface between Chi1 and CBD-B shows that the Chi2CTR occupies a hydrophobic cleft formed by CBD-B, similar to the CBD-A interface. D Structural alignment of TcdA1 (light gray) and YenTc (dark gray) neuraminidase-like domains showing the conserved insertion point of the RBD-B/C (orange and red) daisy chain and CBD-B domain (green), respectively. When superimposed into the YenTc prepore map, the CBD-B domain is rotated 107° downward compared to the positioning of RBD-B/C in TcdA1.

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