PDBsum entry 4d5a

Hydrolase

PDB id: 4d5a

Contents

Protein chains

406 a.a.

Ligands

PGE ×8

GOL ×4

Metals

_CA ×4

Waters ×791

References listed in PDB file

Key reference

• Title: Cwp84, A clostridium difficile cysteine protease, Exhibits conformational flexibility in the absence of its propeptide.
• Authors: W.J.Bradshaw, A.K.Roberts, C.C.Shone, K.R.Acharya.
• Ref.: Acta Crystallogr F Struct Biol Commun, 2015, 71, 295-303. [DOI no: 10.1107/S2053230X15001065]
• PubMed id: 25760704

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.