Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis

Furlong, E.J.; Kurth, F.; Premkumar, L.; Whitten, A.E.; Martin, J.L.

doi:10.1107/S2059798319000081

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 1
Schematic representation of the PmScsC variants used in this study. The region corresponding to the catalytic domain is shown in green, the trimerization stem is coloured magenta and the region representing the flexible linker is shown in cyan. The orange circles represent the approximate positions of the redox-active cysteines.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 75| Part 3| March 2019| Pages 296-307

https://doi.org/10.1107/S2059798319000081

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