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:
The FEBS journal
影响因子:
--
通讯作者:
Acharya KR
Acharya KR
中科院分区:
其他
文献类型:
--
作者:
Bradshaw WJ;Kirby JM;Roberts AK;Shone CC;Acharya KR

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艰难梭菌是世界各地医疗保健系统的负担,每年造成数万人死亡。细菌的S层是细胞表面发现的一层蛋白质,在过去的二十年里受到了大量的关注,作为对抗C.艰难感染。S层包含多种蛋白质,每种蛋白质都具有三个细胞壁结合结构域,而许多蛋白质还具有“功能”区域。在这里,我们提出了一个这样的蛋白质,Cwp19沿着与预测的糖苷水解酶的初步功能表征的功能区域的高分辨率结构。Cwp19具有TIM桶折叠,并且似乎具有高度的底物选择性。该蛋白还表现出肽聚糖水解酶活性,比溶菌酶慢一个数量级,是糖苷水解酶样家族10的第一个成员。这项研究有助于理解Cwp19在C的S层中的作用。很难结构数据可在PDB中以登录号5OQ2和5OQ3获得。
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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