 |
PDBsum entry 5oq3
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
The molecular structure of the glycoside hydrolase domain of cwp19 from clostridium difficile.
|
|
|
Authors
|
|
W.J.Bradshaw,
J.M.Kirby,
A.K.Roberts,
C.C.Shone,
K.R.Acharya.
|
|
|
Ref.
|
|
FEBS J, 2017,
284,
4343-4357.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
