6AS9

Filamentous Assembly of Green Fluorescent Protein Supported by a C-terminal fusion of 18-residues, viewed in space group P212121 form 2

6AS9 の概要

• エントリーDOI: 10.2210/pdb6as9/pdb
• 関連するPDBエントリー: 5HBD 5HGE 5HW9
• 分子名称: Green fluorescent protein, ACETATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: filament, protofilament, 2 sub 1 screw symmetry, protein fibril
• 由来する生物種: Aequorea victoria (Jellyfish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29305.06

構造登録者

Sawaya, M.R.,Heller, D.M.,McPartland, L.,Hochschild, A.,Eisenberg, D.S. (登録日: 2017-08-23, 公開日: 2018-05-30, 最終更新日: 2026-03-18)

主引用文献

McPartland, L.,Heller, D.M.,Eisenberg, D.S.,Hochschild, A.,Sawaya, M.R.
Atomic insights into the genesis of cellular filaments by globular proteins.
Nat. Struct. Mol. Biol., 25:705-714, 2018

PubMed Abstract: Self-assembly of proteins into filaments, such as actin and tubulin filaments, underlies essential cellular processes in all three domains of life. The early emergence of filaments in evolutionary history suggests that filament genesis might be a robust process. Here we describe the fortuitous construction of GFP fusion proteins that self-assemble as fluorescent polar filaments in Escherichia coli. Filament formation is achieved by appending as few as 12 residues to GFP. Crystal structures reveal that each protomer donates an appendage to fill a groove between the two following protomers along the filament. This exchange of appendages resembles runaway domain swapping but is distinguished by higher efficiency because monomers cannot competitively bind their own appendages. Ample evidence for this 'runaway domain coupling' mechanism in nature suggests it could facilitate the evolutionary pathway from globular protein to polar filament, requiring a minimal extension of protein sequence and no substantial refolding.

PubMed: 30076408
DOI: 10.1038/s41594-018-0096-7

実験手法

X-RAY DIFFRACTION (1.75 Å)