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  • The EMBO Journal (2004) 23, 701 - 711
  • doi:10.1038/sj.emboj.7600100

Published online: 5 February 2004

The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel bold beta-roll

Heli Nummelin1, Michael C Merckel6, Jack C Leo1, Hilkka Lankinen2, Mikael Skurnik3,4,5 and Adrian Goldman1

  1. Macromolecular X-ray Crystallography Group, Institute of Biotechnology, University of Helsinki, Helsinki, Finland
  2. Department of Virology, Haartman Institute, University of Helsinki, Finland
  3. Department of Bacteriology and Immunology, Haartman Institute, University of Helsinki, Helsinki, Finland
  4. Helsinki University Central Hospital Laboratory Diagnostics, University of Helsinki, Helsinki, Finland
  5. Department of Medical Biochemistry and Molecular Biology, University of Turku, Turku, Finland
  6. Helsinki Bioenergetics Group, Institute of Biotechnology, University of Helsinki, Helsinki, Finland

Correspondence to:

Adrian Goldman, Institute of Biotechnology, Biocenter, Structural Biology, University of Helsinki, Viikinkaari 1, FIN-00710 Helsinki, Finland. Tel.: +358 9 191 58923; Fax: +358 9 191 59940; E-mail: adrian.goldman@helsinki.fi

Received 6 June 2003; Accepted 5 January 2004

The crystal structure of the recombinant collagen-binding domain of Yersinia adhesin YadA from Yersinia enterocolitica serotype O:3 was solved at 1.55 Å resolution. The trimeric structure is composed of head and neck regions, and the collagen binding head region is a novel nine-coiled left-handed parallel beta-roll. Before the beta-roll, the polypeptide loops from one monomer to the rest, and after the beta-roll the neck region does the same, making the transition from the globular head region to the narrower stalk domain. This creates an intrinsically stable 'lock nut' structure. The trimeric form of YadA is required for collagen binding, and mutagenesis of its surface residues allowed identification of a putative collagen-binding surface. Furthermore, a new structure–sequence motif for YadA beta-roll was used to identify putative YadA-head-like domains in a variety of human and plant pathogens. Such domains may therefore be a common bacterial strategy for avoiding host response.

  • Keywords:

    • adhesin,
    • collagen binding,
    • MAD phasing,
    • X-ray crystallography,
    • YadA