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

Figure 2
Ribbon and surface comparisons between the overall structures before and after propeptide cleavage. The domains are coloured in the same way as in Fig. 1

. Gln110, C116A and His262 are shown as sticks in the ribbon diagrams and in pink in the surface representations. The calcium ion bound to the lectin-like domain is shown in orange. The three loops that undergo conformational changes are circled. 1, Met160–Ser164; 2, Leu315–Asp320; 3, Thr479–Pro485. (a, b) The previously reported structure. The propeptide interacts with both the lectin-like domain, occluding the hydrophobic pocket, and the cysteine protease domain, inserting into the active-site groove. (c, d) The same structure, but with the propeptide graphically removed, showing the shape of the active-site groove when the propeptide is bound. (e, f) Structure 1. Without the propeptide, the structure is largely unchanged except for two loops forming part of the central active-site groove; the significantly smaller S₂ pocket is particularly notable. (g, h) The two loops in structure 2 assume the same conformation as in structure 1, while a third loop on the surface of the lectin-like domain has a vastly different conformation, exposing the hydrophobic pocket.

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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