title: Structural and functional features of a collagen-binding matrix protein from the mussel byssus.
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.
authors.affiliation: 1] Lehrstuhl Biomaterialien, Fakultät für Ingenieurwissenschaften, Universität Bayreuth, Universitätsstraße 30, Bayreuth 95440, Germany [2].
authors.forename: Michael H
authors.initials: MH
authors.lastname: Suhre
authors.affiliation: 1] Lehrstuhl Biochemie, Fakultät für Biologie, Chemie und Geowissenschaften, Universität Bayreuth, Universitätsstraße 30, Bayreuth 95440, Germany [2].
authors.forename: Melanie
authors.initials: M
authors.lastname: Gertz
authors.affiliation: 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.
authors.forename: Clemens
authors.initials: C
authors.lastname: Steegborn
authors.affiliation: 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.
authors.forename: Thomas
authors.initials: T
authors.lastname: Scheibel
mesh_terms: D000595:Amino Acid Sequence; D000825:Animal Structures / Q000378:metabolism; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D049872:Bivalvia / Q000235:genetics / Q000378:metabolism*; D002942:Circular Dichroism; D003094:Collagen / Q000378:metabolism*; D018360:Crystallography, X-Ray; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D058767:Protein Unfolding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
chemical_list: D011506:Proteins; D003094:Collagen