4CN8
Structure of proximal thread matrix protein 1 (PTMP1) from the mussel byssus
Summary for 4CN8
| Entry DOI | 10.2210/pdb4cn8/pdb |
| Related | 4CN9 4CNB |
| Descriptor | PROXIMAL THREAD MATRIX PROTEIN 1, 1,2-ETHANEDIOL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | structural protein |
| Biological source | MYTILUS GALLOPROVINCIALIS (MEDITERRANEAN MUSSEL) |
| Total number of polymer chains | 1 |
| Total formula weight | 49423.69 |
| Authors | Gertz, M.,Suhre, M.H.,Scheibel, T.,Steegborn, C. (deposition date: 2014-01-21, release date: 2014-03-12, Last modification date: 2024-11-20) |
| Primary citation | Suhre, M.H.,Gertz, M.,Steegborn, C.,Scheibel, T. Structural and Functional Features of a Collagen-Binding Matrix Protein from the Mussel Byssus. Nat.Commun., 5:3392-, 2014 Cited by PubMed 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. PubMed: 24569701DOI: 10.1038/NCOMMS4392 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
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