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PDBsum entry 2yl5
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References listed in PDB file
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Key reference
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Title
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Inhibition of the pneumococcal virulence factor strh and molecular insights into n-Glycan recognition and hydrolysis.
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Authors
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B.Pluvinage,
M.A.Higgins,
D.W.Abbott,
C.Robb,
A.B.Dalia,
L.Deng,
J.N.Weiser,
T.B.Parsons,
A.J.Fairbanks,
D.J.Vocadlo,
A.B.Boraston.
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Ref.
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Structure, 2011,
19,
1603-1614.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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The complete degradation of N-linked glycans by the pathogenic bacterium
Streptococcus pneumoniae is facilitated by the large multimodular cell
wall-attached exo-β-D-N-acetylglucosaminidase StrH. Structural dissection of
this virulence factor using X-ray crystallography showed it to have two
structurally related glycoside hydrolase family 20 catalytic domains, which
displayed the expected specificity for complex N-glycans terminating in
N-acetylglucosamine but exhibited unexpected differences in their preferences
for the substructures present in these glycans. The structures of the two
catalytic domains in complex with unhydrolyzed substrates, including an N-glycan
possessing a bisecting N-acetylglucosamine residue, revealed the specific
architectural features in the active sites that confer their differential
specificities. Inhibitors of StrH are demonstrated to be effective tools in
modulating the interaction of StrH with components of the host, such as the
innate immune system. Overall, new structural and functional insight into a
carbohydrate-mediated component of the pneumococcus-host interaction is provided.
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