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Defining the structural basis of human plasminogen binding by streptococcal surface enolase.

Abstract:

The flesh-eating bacterium group A Streptococcus (GAS) binds and activates human plasminogen, promoting invasive disease. Streptococcal surface enolase (SEN), a glycolytic pathway enzyme, is an identified plasminogen receptor of GAS. Here we used mass spectrometry (MS) to confirm that GAS SEN is octameric, thereby validating in silico modeling based on the crystal structure of Streptococcus pneumoniae alpha-enolase. Site-directed mutagenesis of surface-located lysine residues (SEN(K252 + 255A...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m109.004317

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Journal:
The Journal of biological chemistry
Volume:
284
Issue:
25
Pages:
17129-17137
Publication date:
2009-06-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:8a3b6803-b6cb-48ab-961d-ff401f66955d
Source identifiers:
59400
Local pid:
pubs:59400

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