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6MDR

Cryo-EM structure of the Ceru+32/GFP-17 protomer

6MDR の概要
エントリーDOI10.2210/pdb6mdr/pdb
EMDBエントリー9104
分子名称Ceru+32, GFP-17 (2 entities in total)
機能のキーワードsupercharged protein assembly, electrostatic interactions, 16-mer, d4 symmetry, luminescent protein
由来する生物種Aequorea victoria (Jellyfish)
詳細
タンパク質・核酸の鎖数16
化学式量合計445211.50
構造登録者
主引用文献Simon, A.J.,Zhou, Y.,Ramasubramani, V.,Glaser, J.,Pothukuchy, A.,Gollihar, J.,Gerberich, J.C.,Leggere, J.C.,Morrow, B.R.,Jung, C.,Glotzer, S.C.,Taylor, D.W.,Ellington, A.D.
Supercharging enables organized assembly of synthetic biomolecules.
Nat Chem, 11:204-212, 2019
Cited by
PubMed Abstract: Symmetrical protein oligomers are ubiquitous in biological systems and perform key structural and regulatory functions. However, there are few methods for constructing such oligomers. Here we have engineered completely synthetic, symmetrical oligomers by combining pairs of oppositely supercharged variants of a normally monomeric model protein through a strategy we term 'supercharged protein assembly' (SuPrA). We show that supercharged variants of green fluorescent protein can assemble into a variety of architectures including a well-defined symmetrical 16-mer structure that we solved using cryo-electron microscopy at 3.47 Å resolution. The 16-mer is composed of two stacked rings of octamers, in which the octamers contain supercharged proteins of alternating charges, and interactions within and between the rings are mediated by a variety of specific electrostatic contacts. The ready assembly of this structure suggests that combining oppositely supercharged pairs of protein variants may provide broad opportunities for generating novel architectures via otherwise unprogrammed interactions.
PubMed: 30643229
DOI: 10.1038/s41557-018-0196-3
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.47 Å)
構造検証レポート
Validation report summary of 6mdr
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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