7OOM

N-terminal domain of FlSp spidroin from Nephila clavipes

7OOM の概要

• エントリーDOI: 10.2210/pdb7oom/pdb
• 分子名称: Flagelliform spidroin variant 1 (2 entities in total)
• 機能のキーワード: spider silk, spidroin, structural protein
• 由来する生物種: Nephila clavipes (Golden silk orbweaver)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28513.23

構造登録者

Tars, K.,Metlans, R.,Fridmanis, J.,Jaudzems, K. (登録日: 2021-05-28, 公開日: 2022-06-08, 最終更新日: 2024-06-19)

主引用文献

Sarr, M.,Kitoka, K.,Walsh-White, K.A.,Kaldmae, M.,Metlans, R.,Tars, K.,Mantese, A.,Shah, D.,Landreh, M.,Rising, A.,Johansson, J.,Jaudzems, K.,Kronqvist, N.
The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence.
J.Biol.Chem., 298:101913-101913, 2022

PubMed Abstract: The N-terminal (NT) domain of spider silk proteins (spidroins) is crucial for their storage at high concentrations and also regulates silk assembly. NTs from the major ampullate spidroin (MaSp) and the minor ampullate spidroin are monomeric at neutral pH and confer solubility to spidroins, whereas at lower pH, they dimerize to interconnect spidroins in a fiber. This dimerization is known to result from modulation of electrostatic interactions by protonation of well-conserved glutamates, although it is undetermined if this mechanism applies to other spidroin types as well. Here, we determine the solution and crystal structures of the flagelliform spidroin NT, which shares only 35% identity with MaSp NT, and investigate the mechanisms of its dimerization. We show that flagelliform spidroin NT is structurally similar to MaSp NT and that the electrostatic intermolecular interaction between Asp 40 and Lys 65 residues is conserved. However, the protonation events involve a different set of residues than in MaSp, indicating that an overall mechanism of pH-dependent dimerization is conserved but can be mediated by different pathways in different silk types.

PubMed: 35398358
DOI: 10.1016/j.jbc.2022.101913

実験手法

X-RAY DIFFRACTION (1.8 Å)