5OQ3

High resolution structure of the functional region of Cwp19 from Clostridium difficile

5OQ3 の概要

• エントリーDOI: 10.2210/pdb5oq3/pdb
• 分子名称: Cwp19, CHLORIDE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: s-layer, glycoside hydrolase, tim barrel, hydrolase
• 由来する生物種: Clostridioides difficile
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45039.73

構造登録者

Bradshaw, W.J.,Kirby, J.M.,Roberts, A.K.,Shone, C.C.,Acharya, K.R. (登録日: 2017-08-10, 公開日: 2017-11-01, 最終更新日: 2024-01-17)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.35 Å)