2KHM

Structure of the C-terminal non-repetitive domain of the spider dragline silk protein ADF-3

2KHM の概要

• エントリーDOI: 10.2210/pdb2khm/pdb
• NMR情報: BMRB: 16249
• 分子名称: Fibroin-3 (1 entity in total)
• 機能のキーワード: alpha helix, homodimer, swapped, structural protein
• 由来する生物種: Araneus diadematus (Spider)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26659.48

構造登録者

Hagn, F.X.,Eisoldt, L.,Hardy, J.G.,Vendrely, C.,Coles, M.,Scheibel, T.,Kessler, H. (登録日: 2009-04-09, 公開日: 2010-04-14, 最終更新日: 2024-11-20)

主引用文献

Hagn, F.,Eisoldt, L.,Hardy, J.G.,Vendrely, C.,Coles, M.,Scheibel, T.,Kessler, H.
A conserved spider silk domain acts as a molecular switch that controls fibre assembly
Nature, 465:239-242, 2010

PubMed Abstract: A huge variety of proteins are able to form fibrillar structures, especially at high protein concentrations. Hence, it is surprising that spider silk proteins can be stored in a soluble form at high concentrations and transformed into extremely stable fibres on demand. Silk proteins are reminiscent of amphiphilic block copolymers containing stretches of polyalanine and glycine-rich polar elements forming a repetitive core flanked by highly conserved non-repetitive amino-terminal and carboxy-terminal domains. The N-terminal domain comprises a secretion signal, but further functions remain unassigned. The C-terminal domain was implicated in the control of solubility and fibre formation initiated by changes in ionic composition and mechanical stimuli known to align the repetitive sequence elements and promote beta-sheet formation. However, despite recent structural data, little is known about this remarkable behaviour in molecular detail. Here we present the solution structure of the C-terminal domain of a spider dragline silk protein and provide evidence that the structural state of this domain is essential for controlled switching between the storage and assembly forms of silk proteins. In addition, the C-terminal domain also has a role in the alignment of secondary structural features formed by the repetitive elements in the backbone of spider silk proteins, which is known to be important for the mechanical properties of the fibre.

PubMed: 20463741
DOI: 10.1038/nature08936

実験手法

SOLUTION NMR