Modelling of steric structure of a periplasmic molecular chaperone Caf1M of Yersinia pestis, a prototype member of a subfamily with characteristic structural and functional features.

@article{Zavyalov1995ModellingOS,
  title={Modelling of steric structure of a periplasmic molecular chaperone Caf1M of Yersinia pestis, a prototype member of a subfamily with characteristic structural and functional features.},
  author={Vladimir P. Zav'yalov and Galina A. Zav'yalova and Alexander I. Denesyuk and Timo Korpela},
  journal={FEMS immunology and medical microbiology},
  year={1995},
  volume={11 1},
  pages={19-24}
}
Steric structure of Caf1M, a periplasmic molecular chaperone of Yersinia pestis, was reconstructed by computer modelling based on a statistically significant primary structure homology between Caf1M and PapD protein from Escherichia coli, and using the known atomic coordinates obtained by the X-ray crystallography for PapD. In the three-dimensional model of Caf1M an accessory sequence between F1 and G1 beta-strands (as compared to PapD) can form a strain-specific part of the binding pocket of… CONTINUE READING