4D5A

Clostridial Cysteine protease Cwp84 C116A after propeptide cleavage

Summary for 4D5A

• Entry DOI: 10.2210/pdb4d5a/pdb
• Related: 4D59
• Descriptor: CELL SURFACE PROTEIN (PUTATIVE CELL SURFACE-ASSOCIATED CYSTEINE PROTEASE), CALCIUM ION, TRIETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: hydrolase, s-layer, surface layer
• Biological source: PEPTOCLOSTRIDIUM DIFFICILE
• Total number of polymer chains: 2
• Total formula weight: 91927.81

Authors

Bradshaw, W.J.,Roberts, A.K.,Shone, C.C.,Acharya, K.R. (deposition date: 2014-11-03, release date: 2015-03-04, Last modification date: 2023-12-20)

Primary citation

Bradshaw, W.J.,Roberts, A.K.,Shone, C.C.,Acharya, K.R.
Cwp84, a Clostridium Difficile Cysteine Protease, Exhibits Conformational Flexibility in the Absence of its Propeptide
Acta Crystallogr.,Sect.F, 71:295-, 2015

PubMed 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.

PubMed: 25760704
DOI: 10.1107/S2053230X15001065

Experimental method

X-RAY DIFFRACTION (1.6 Å)