5OQ2

Se-SAD structure of the functional region of Cwp19 from Clostridium difficile

Summary for 5OQ2

• Entry DOI: 10.2210/pdb5oq2/pdb
• Descriptor: Cwp19, PHOSPHATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: s-layer, glycoside hydrolase, tim barrel, hydrolase
• Biological source: Clostridioides difficile
• Total number of polymer chains: 2
• Total formula weight: 90486.92

Authors

Bradshaw, W.J.,Kirby, J.M.,Roberts, A.K.,Shone, C.C.,Acharya, K.R. (deposition date: 2017-08-10, release date: 2017-11-01, Last modification date: 2024-11-20)

Primary citation

Bradshaw, W.J.,Kirby, J.M.,Roberts, A.K.,Shone, C.C.,Acharya, K.R.
The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile.
FEBS J., 284:4343-4357, 2017

PubMed Abstract: Clostridium difficile is a burden to healthcare systems around the world, causing tens of thousands of deaths annually. The S-layer of the bacterium, a layer of protein found of the surface of cells, has received a significant amount of attention over the past two decades as a potential target to combat the growing threat presented by C. difficile infections. The S-layer contains a wide range of proteins, each of which possesses three cell wall-binding domains, while many also possess a "functional" region. Here, we present the high resolution structure of the functional region of one such protein, Cwp19 along with preliminary functional characterisation of the predicted glycoside hydrolase. Cwp19 has a TIM barrel fold and appears to possess a high degree of substrate selectivity. The protein also exhibits peptidoglycan hydrolase activity, an order of magnitude slower than that of lysozyme and is the first member of glycoside hydrolase-like family 10 to be characterised. This research goes some way to understanding the role of Cwp19 in the S-layer of C. difficile.

PubMed: 29083543
DOI: 10.1111/febs.14310

Experimental method

X-RAY DIFFRACTION (2.3 Å)