Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide

Bradshaw, W.J.; Roberts, A.K.; Shone, C.C.; Acharya, K.R.

doi:10.1107/S2053230X15001065

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
Calcium displacement of Lys108. Distances are given in Å. (a) The previously determined structure with the propeptide. Several negatively charged moieties bind to Lys108. (b) Structure 1 exhibits the same conformation as that with the propeptide. (c) In structure 2, Lys108 is displaced by a calcium ion. Coordination of the calcium ion is slightly tighter, but this does not result in any significant changes to the fold; notably, the nearby catalytic residues are unaffected.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 71| Part 3| March 2015| Pages 295-303

https://doi.org/10.1107/S2053230X15001065

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