An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase

Wong, J.E.M.M.; Midtgaard, S.R.; Gysel, K.; Thygesen, M.B.; Sørensen, K.K.; Jensen, K.J.; Stougaard, J.; Thirup, S.; Blaise, M.

doi:10.1107/S139900471402793X

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 8
Comparison of the relative positions of the LysM2 domains in the three crystal structures. The figure shows that the linker between the two LysM domains confers flexibility between LysM domains. The positions of the LysM2 domains from full-length P60_tth (grey), P60_2LysM bound to chitohexaose (green) and P60_2LysM free from ligand (blue) are compared.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 71| Part 3| February 2015| Pages 592-605

doi:10.1107/S139900471402793X

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