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

William J. Bradshaw, April K. Roberts, Clifford C. Shone, K. Ravi Acharya

Research output: Contribution to journalArticle

5 Citations (Scopus)
91 Downloads (Pure)

Abstract

In recent decades, the global healthcare problems caused by Clostridium difficile have increased at an alarming rate. A greater understanding of this antibiotic-resistant bacterium, particularly with respect to how it interacts with the host, is required for the development of novel strategies for fighting C. difficile infections. The surface layer (S-layer) of C. difficile is likely to be of significant importance to host-pathogen interactions. The mature S-layer is formed by a proteinaceous array consisting of multiple copies of a high-molecular-weight and a low-molecular-weight S-layer protein. These components result from the cleavage of SlpA by Cwp84, a cysteine protease. The structure of a truncated Cwp84 active-site mutant has recently been reported and the key features have been identified, providing the first structural insights into the role of Cwp84 in the formation of the S-layer. Here, two structures of Cwp84 after propeptide cleavage are presented and the three conformational changes that are observed are discussed. These changes result in a reconfiguration of the active site and exposure of the hydrophobic pocket.

Original languageEnglish
Pages (from-to)295-303
Number of pages9
JournalActa Crystallographica Section F:Structural Biology Communications
Volume71
DOIs
Publication statusPublished - 1 Mar 2015

Keywords

  • Clostridium difficile
  • Cwp84
  • host-pathogen interactions
  • surface layer

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