Journal article
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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Authors
Bibliographic Details
- Journal:
- Journal of biological chemistry
- Volume:
- 284
- Issue:
- 25
- Pages:
- 17129-17137
- Publication date:
- 2009-06-01
- DOI:
- EISSN:
-
1083-351X
- ISSN:
-
0021-9258
- Source identifiers:
-
59400
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:59400
- UUID:
-
uuid:8a3b6803-b6cb-48ab-961d-ff401f66955d
- Local pid:
- pubs:59400
- Deposit date:
- 2012-12-19
Terms of use
- Copyright date:
- 2009
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