Crystal structures of the GH18 domain of the bifunctional peroxiredoxin–chitinase CotE from Clostridium difficile

Whittingham, J.L.; Hanai, S.; Brannigan, J.A.; Ferreira, W.T.; Dodson, E.J.; Turkenburg, J.P.; Cartwright, J.; Cutting, S.M.; Wilkinson, A.J.

doi:10.1107/S2053230X20006147

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
Domain swapping in the chitinase domain of CotE. (a) Ribbon rendering of the chitinase domain in the P6₁22 crystal structure. The chain is colour-ramped as in Fig. 1

(a), and the C^α atoms and side chains of cysteines 376 and 670 are shown as spheres. The C-terminal residues 627–712 extend away from the β-barrel so as to pack onto and complete the β-barrel of a crystallographic symmmetry mate, as shown in (c), where the two subunits of the domain-swapped dimer are coloured light blue and green, respectively. The eighth strand of each β-barrel is provided by the partner subunit. (b) A juxtaposition of the C-terminal swapped domains (residues 627–712) in the P2₁ and P6₁22 crystal forms, coloured light green and ice blue, respectively, relative to the β-barrel domain (in white) following the superposition of residues 358–623 is shown.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 76| Part 6| June 2020| Pages 241-249

https://doi.org/10.1107/S2053230X20006147

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