6HQE

Cryo-EM of self-assembly peptide filament LRV_M3delta1

6HQE の概要

• エントリーDOI: 10.2210/pdb6hqe/pdb
• EMDBエントリー: 0252
• 分子名称: peptide LRV_M3delta1 (1 entity in total)
• 機能のキーワード: filament, self-assembly peptide filament, cryo-em, protein fibril
• 由来する生物種: Azotobacter vinelandii
• タンパク質・核酸の鎖数: 52
• 化学式量合計: 134156.52

構造登録者

Osinski, T.,Wang, F.,Hughes, S.A.,Kreutzberger, M.A.B.,Conticello, V.P.,Egelman, E.H. (登録日: 2018-09-24, 公開日: 2019-06-26, 最終更新日: 2024-05-15)

主引用文献

Hughes, S.A.,Wang, F.,Wang, S.,Kreutzberger, M.A.B.,Osinski, T.,Orlova, A.,Wall, J.S.,Zuo, X.,Egelman, E.H.,Conticello, V.P.
Ambidextrous helical nanotubes from self-assembly of designed helical hairpin motifs.
Proc.Natl.Acad.Sci.USA, 116:14456-14464, 2019

PubMed Abstract: Tandem repeat proteins exhibit native designability and represent potentially useful scaffolds for the construction of synthetic biomimetic assemblies. We have designed 2 synthetic peptides, HEAT_R1 and LRV_M3Δ1, based on the consensus sequences of single repeats of thermophilic HEAT (PBS_HEAT) and Leucine-Rich Variant (LRV) structural motifs, respectively. Self-assembly of the peptides afforded high-aspect ratio helical nanotubes. Cryo-electron microscopy with direct electron detection was employed to analyze the structures of the solvated filaments. The 3D reconstructions from the cryo-EM maps led to atomic models for the HEAT_R1 and LRV_M3Δ1 filaments at resolutions of 6.0 and 4.4 Å, respectively. Surprisingly, despite sequence similarity at the lateral packing interface, HEAT_R1 and LRV_M3Δ1 filaments adopt the opposite helical hand and differ significantly in helical geometry, while retaining a local conformation similar to previously characterized repeat proteins of the same class. The differences in the 2 filaments could be rationalized on the basis of differences in cohesive interactions at the lateral and axial interfaces. These structural data reinforce previous observations regarding the structural plasticity of helical protein assemblies and the need for high-resolution structural analysis. Despite these observations, the native designability of tandem repeat proteins offers the opportunity to engineer novel helical nanotubes. Moreover, the resultant nanotubes have independently addressable and chemically distinguishable interior and exterior surfaces that would facilitate applications in selective recognition, transport, and release.

PubMed: 31262809
DOI: 10.1073/pnas.1903910116

実験手法

ELECTRON MICROSCOPY (4.4 Å)