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PDBsum entry 4ci7
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References listed in PDB file
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Key reference
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Title
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The structure of the cysteine protease and lectin-Like domains of cwp84, A surface layer-Associated protein from clostridium difficile.
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Authors
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W.J.Bradshaw,
J.M.Kirby,
N.Thiyagarajan,
C.J.Chambers,
A.H.Davies,
A.K.Roberts,
C.C.Shone,
K.R.Acharya.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2014,
70,
1983-1993.
[DOI no: ]
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PubMed id
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Abstract
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Clostridium difficile is a major problem as an aetiological agent for
antibiotic-associated diarrhoea. The mechanism by which the bacterium colonizes
the gut during infection is poorly understood, but undoubtedly involves a myriad
of components present on the bacterial surface. The mechanism of C. difficile
surface-layer (S-layer) biogenesis is also largely unknown but involves the
post-translational cleavage of a single polypeptide (surface-layer protein A;
SlpA) into low- and high-molecular-weight subunits by Cwp84, a surface-located
cysteine protease. Here, the first crystal structure of the surface protein
Cwp84 is described at 1.4 Å resolution and the key structural components are
identified. The truncated Cwp84 active-site mutant (amino-acid residues 33-497;
C116A) exhibits three regions: a cleavable propeptide and a cysteine protease
domain which exhibits a cathepsin L-like fold followed by a newly identified
putative carbohydrate-binding domain with a bound calcium ion, which is referred
to here as a lectin-like domain. This study thus provides the first structural
insights into Cwp84 and a strong base to elucidate its role in the C. difficile
S-layer maturation mechanism.
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