The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile.
The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile.
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DOI:
10.1111/febs.14310
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发表时间:
2017-12
期刊:
影响因子:
--
通讯作者:
Acharya KR
中科院分区:
文献类型:
--
作者:
Bradshaw WJ;Kirby JM;Roberts AK;Shone CC;Acharya KR
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. Structural data are available in the PDB under the accession numbers 5OQ2 and 5OQ3.
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DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
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通讯作者:
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通讯作者:
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影响因子:
2.3
作者:
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