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Collagen-like sequences in phages and bacteria

Engel, Juergen ; Bächinger, Hans

In: Proceedings of the Indian Academy of Sciences - Chemical Sciences, 1999, vol. 111, no. 1, p. 81-86

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    Titre
    • Collagen-like sequences in phages and bacteria
    Auteur
    • Engel, Juergen. Department of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstr. 70, CH-4056, Basel, Switzerland
    • Bächinger, Hans. Research Unit, Shriners Hospital for Children and the Department of Biochemistry and Molecular Biology, Oregon Health Science University, 97201, Portland, Oregon, USA
    Type de document
    • Postprint
    Langue
    • Inglese
    Publié dans
    • Proceedings of the Indian Academy of Sciences - Chemical Sciences, 1999, vol. 111, no. 1, p. 81-86. Springer India
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:315388
    Summary
    Sequences with glycine in every third position have been detected in DNA derived sequences of proteins in phages and bacteria and it was suggested that these regions trimerise to collagenous structures. Related sequences are found in proteins of mollusks and slime mold. The sequences contain a much lower fraction of proline than mammalian collagens and it is unknown how many of the prolines, if any, are converted to hydroxyproline. Therefore, for triple helix formation other stabilizing interactions than those known for mammalian collagens are required. Strikingly, aspartate and asparagine are abundant in collagen-like sequences of phage tail fibre proteins and of related sequences in nacrein of oyster pearls suggesting a possible stabilization by calcium binding