2oto
From Proteopedia
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| , resolution 3.040Å | |||||||
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| Ligands: | |||||||
| Gene: | emm1.0 (Streptococcus pyogenes serotype M1) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
N-terminal fragment of Streptococcus pyogenes M1 protein
Overview
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.
About this Structure
2OTO is a Single protein structure of sequence from Streptococcus pyogenes serotype m1. Full crystallographic information is available from OCA.
Reference
Coiled-coil irregularities and instabilities in group A Streptococcus M1 are required for virulence., McNamara C, Zinkernagel AS, Macheboeuf P, Cunningham MW, Nizet V, Ghosh P, Science. 2008 Mar 7;319(5868):1405-8. PMID:18323455
Page seeded by OCA on Mon Mar 31 04:22:56 2008
