PDBsum entry 4cnb

Structural protein

PDB id: 4cnb

Contents

Protein chains

387 a.a.

Ligands

SO4 ×2

EDO ×3

Waters ×333

PDB id:

4cnb

Name:

Structural protein

Title:

Structure of proximal thread matrix protein 1 (ptmp1) from the mussel byssus - crystal form 2

Structure:

Proximal thread matrix protein 1. Chain: a, b. Engineered: yes

Source:

Mytilus galloprovincialis. Mediterranean mussel. Organism_taxid: 29158. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: ripl.

Resolution:

1.95Å R-factor: 0.216 R-free: 0.254

Authors:

M.Gertz,M.H.Suhre,T.Scheibel,C.Steegborn

Key ref:

M.H.Suhre et al. (2014). Structural and functional features of a collagen-binding matrix protein from the mussel byssus. Nat Commun, 5, 3392. PubMed id: 24569701 DOI: 10.1038/ncomms4392

Date:

21-Jan-14 Release date: 12-Mar-14

Protein chains

Q8T5C2  (Q8T5C2_MYTGA) -  Proximal thread matrix protein 1 from Mytilus galloprovincialis

Seq: 453 a.a.

Struc: 387 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1038/ncomms4392

Nat Commun 5:3392 (2014)

PubMed id: 24569701

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

M.H.Suhre, M.Gertz, C.Steegborn, T.Scheibel.

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.