2OTO
N-terminal fragment of Streptococcus pyogenes M1 protein
Summary for 2OTO
| Entry DOI | 10.2210/pdb2oto/pdb |
| Descriptor | M protein (1 entity in total) |
| Functional Keywords | helical coiled coil, fibrinogen-binding, virulence factor, surface active protein, toxin |
| Biological source | Streptococcus pyogenes serotype M1 |
| Total number of polymer chains | 4 |
| Total formula weight | 72727.67 |
| Authors | McNamara, C.W.,Ghosh, P. (deposition date: 2007-02-08, release date: 2008-03-18, Last modification date: 2024-11-20) |
| Primary citation | McNamara, C.,Zinkernagel, A.S.,Macheboeuf, P.,Cunningham, M.W.,Nizet, V.,Ghosh, P. Coiled-coil irregularities and instabilities in group A Streptococcus M1 are required for virulence. Science, 319:1405-1408, 2008 Cited by PubMed Abstract: Antigenically variable M proteins are major virulence factors and immunogens of the human pathogen group A Streptococcus (GAS). Here, we report the approximately 3 angstrom resolution structure of a GAS M1 fragment containing the regions responsible for eliciting type-specific, protective immunity and for binding fibrinogen, which promotes M1 proinflammatory and antiphagocytic functions. The structure revealed substantial irregularities and instabilities throughout the coiled coil of the M1 fragment. Similar structural irregularities occur in myosin and tropomyosin, explaining the patterns of cross-reactivity seen in autoimmune sequelae of GAS infection. Sequence idealization of a large segment of the M1 coiled coil enhanced stability but diminished fibrinogen binding, proinflammatory effects, and antibody cross-reactivity, whereas it left protective immunogenicity undiminished. Idealized M proteins appear to have promise as vaccine immunogens. PubMed: 18323455DOI: 10.1126/science.1154470 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.04 Å) |
Structure validation
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