The type III secretion chaperone SctY may shield the hydrophobic export gate-binding C-terminus of its substrate SctX

Gilzer, D.; Kowal, J.L.; Flottmann, F.; Niemann, H.H.

doi:10.1107/S2059798323003248

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 6
Crystallographic SctX–Sct′Y tetramers. Tetramerization via the C-terminal helices of SctX was observed in (a) YscX₅₀–YscY (PDB entry 7qih), (b) YscX₃₂–YscY (PDB entry 7qii) and AscX₄₉–YscY (PDB entry 8arb) crystals. The chaperone is colored gray and the substrate is colored cyan, except for the C-terminal 12 residues, which are highlighted in red.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 79| Part 6| June 2023| Pages 508-517

https://doi.org/10.1107/S2059798323003248

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