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PDBsum entry 5oq2
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PDB id:
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Hydrolase
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Title:
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Se-sad structure of the functional region of cwp19 from clostridium difficile
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Structure:
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Cwp19. Chain: a, b. Synonym: n-acetylmuramoyl-l-alanine amidase lytc. Engineered: yes
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Source:
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Clostridioides difficile. Organism_taxid: 1496. Gene: lytc_21, cwp19, lytc_5, samea3374989_00994, samea3375004_02322. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693
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Resolution:
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2.30Å
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R-factor:
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0.196
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R-free:
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0.254
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Authors:
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W.J.Bradshaw,J.M.Kirby,A.K.Roberts,C.C.Shone,K.R.Acharya
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Key ref:
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W.J.Bradshaw
et al.
(2017).
The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile.
FEBS J,
284,
4343-4357.
PubMed id:
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Date:
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10-Aug-17
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Release date:
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01-Nov-17
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PROCHECK
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Headers
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References
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L7PGA3
(L7PGA3_CLODI) -
Cell surface protein from Clostridioides difficile
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Seq:
Struc:
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703 a.a.
360 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class:
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E.C.3.5.1.28
- N-acetylmuramoyl-L-alanine amidase.
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Reaction:
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Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain bacterial cell-wall glycopeptides.
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FEBS J
284:4343-4357
(2017)
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PubMed id:
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The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile.
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W.J.Bradshaw,
J.M.Kirby,
A.K.Roberts,
C.C.Shone,
K.R.Acharya.
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ABSTRACT
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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.
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