Structural highlights
Publication Abstract from PubMedIn 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. Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide.,Bradshaw WJ, Roberts AK, Shone CC, Acharya KR Acta Crystallogr F Struct Biol Commun. 2015 Mar 1;71(Pt 3):295-303. doi:, 10.1107/S2053230X15001065. Epub 2015 Feb 19. PMID:25760704[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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