7LIL

Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3

7LIL の概要

• エントリーDOI: 10.2210/pdb7lil/pdb
• EMDBエントリー: 23379 23380 23381 23382 23383 23384 23385
• 分子名称: Maritimacin, RIBOFLAVIN (2 entities in total)
• 機能のキーワード: encapsulin, nanocompartment, virus like particle
• 由来する生物種: Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30922.12

構造登録者

Andreas, M.P.,Adamson, L.,Tasneem, N.,Close, W.,Giessen, T.,Lau, Y.H. (登録日: 2021-01-27, 公開日: 2022-02-09, 最終更新日: 2024-05-29)

主引用文献

Adamson, L.S.R.,Tasneem, N.,Andreas, M.P.,Close, W.,Jenner, E.N.,Szyszka, T.N.,Young, R.,Cheah, L.C.,Norman, A.,MacDermott-Opeskin, H.I.,O'Mara, M.L.,Sainsbury, F.,Giessen, T.W.,Lau, Y.H.
Pore structure controls stability and molecular flux in engineered protein cages.
Sci Adv, 8:eabl7346-eabl7346, 2022

PubMed Abstract: Protein cages are a common architectural motif used by living organisms to compartmentalize and control biochemical reactions. While engineered protein cages have featured in the construction of nanoreactors and synthetic organelles, relatively little is known about the underlying molecular parameters that govern stability and flux through their pores. In this work, we systematically designed 24 variants of the encapsulin cage, featuring pores of different sizes and charges. Twelve pore variants were successfully assembled and purified, including eight designs with exceptional thermal stability. While negatively charged mutations were better tolerated, we were able to form stable assemblies covering a full range of pore sizes and charges, as observed in seven new cryo-EM structures at 2.5- to 3.6-Å resolution. Molecular dynamics simulations and stopped-flow experiments revealed the importance of considering both pore size and charge, together with flexibility and rate-determining steps, when designing protein cages for controlling molecular flux.

PubMed: 35119930
DOI: 10.1126/sciadv.abl7346

実験手法

ELECTRON MICROSCOPY (2.84 Å)