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Nat Commun. 2014 Feb 26;5:3392. doi: 10.1038/ncomms4392.

Structural and functional features of a collagen-binding matrix protein from the mussel byssus.

Author information

1
1] Lehrstuhl Biomaterialien, Fakultät für Ingenieurwissenschaften, Universität Bayreuth, Universitätsstraße 30, Bayreuth 95440, Germany [2].
2
1] Lehrstuhl Biochemie, Fakultät für Biologie, Chemie und Geowissenschaften, Universität Bayreuth, Universitätsstraße 30, Bayreuth 95440, Germany [2].
3
1] Lehrstuhl Biochemie, Fakultät für Biologie, Chemie und Geowissenschaften, Universität Bayreuth, Universitätsstraße 30, Bayreuth 95440, Germany [2] Institut für Bio-Makromoleküle (bio-mac), Universität Bayreuth, Universitätsstraße 30, Bayreuth 95440, Germany [3] Bayreuther Zentrum für Molekulare Biowissenschaften (BZMB), Universität Bayreuth, Universitätsstraße 30, Bayreuth 95440, Germany.
4
1] Lehrstuhl Biomaterialien, Fakultät für Ingenieurwissenschaften, Universität Bayreuth, Universitätsstraße 30, Bayreuth 95440, Germany [2] Institut für Bio-Makromoleküle (bio-mac), Universität Bayreuth, Universitätsstraße 30, Bayreuth 95440, Germany [3] Bayreuther Zentrum für Molekulare Biowissenschaften (BZMB), Universität Bayreuth, Universitätsstraße 30, Bayreuth 95440, Germany [4] Bayreuther Zentrum für Kolloide und Grenzflächen (BZKG), Universität Bayreuth, Universitätsstraße 30, Bayreuth 95440, Germany [5] Bayreuther Materialzentrum (BayMAT), Universität Bayreuth, Universitätsstraße 30, Bayreuth 95440, Germany.

Abstract

Blue mussels adhere to surfaces by the byssus, a holdfast structure composed of individual threads representing a collagen fibre reinforced composite. Here, we present the crystal structure and function of one of its matrix proteins, the proximal thread matrix protein 1, which is present in the proximal section of the byssus. The structure reveals two von Willebrand factor type A domains linked by a two-β-stranded linker yielding a novel structural arrangement. In vitro, the protein binds heterologous collagens with high affinity and affects collagen assembly, morphology and arrangement of its fibrils. By providing charged surface clusters as well as insufficiently coordinated metal ions, the proximal thread matrix protein 1 might interconnect other byssal proteins and thereby contribute to the integrity of the byssal threads in vivo. Moreover, the protein could be used for adjusting the mechanical properties of collagen materials, a function likely important in the natural byssus.

PMID:
24569701
DOI:
10.1038/ncomms4392
[Indexed for MEDLINE]

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