3DKT

Crystal structure of Thermotoga maritima encapsulin

3DKT の概要

• エントリーDOI: 10.2210/pdb3dkt/pdb
• 分子名称: Maritimacin, Putative uncharacterized protein (3 entities in total)
• 機能のキーワード: enzyme encapsulation, nanocompartment, oxidative stress, ferritin-like protein, hk97-fold, antibiotic, antimicrobial, bacteriocin, cobalt, hydrolase, protease, secreted, structural protein-virus like particle complex, structural protein/virus like particle
• 由来する生物種: Thermotoga maritima; 詳細
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 313337.35

構造登録者

Sutter, M.,Boehringer, D.,Gutmann, S.,Weber-Ban, E.,Ban, N. (登録日: 2008-06-26, 公開日: 2008-09-02, 最終更新日: 2024-03-20)

主引用文献

Sutter, M.,Boehringer, D.,Gutmann, S.,Gunther, S.,Prangishvili, D.,Loessner, M.J.,Stetter, K.O.,Weber-Ban, E.,Ban, N.
Structural basis of enzyme encapsulation into a bacterial nanocompartment
Nat.Struct.Mol.Biol., 15:939-947, 2008

PubMed Abstract: Compartmentalization is an important organizational feature of life. It occurs at varying levels of complexity ranging from eukaryotic organelles and the bacterial microcompartments, to the molecular reaction chambers formed by enzyme assemblies. The structural basis of enzyme encapsulation in molecular compartments is poorly understood. Here we show, using X-ray crystallographic, biochemical and EM experiments, that a widespread family of conserved bacterial proteins, the linocin-like proteins, form large assemblies that function as a minimal compartment to package enzymes. We refer to this shell-forming protein as 'encapsulin'. The crystal structure of such a particle from Thermotoga maritima determined at 3.1-angstroms resolution reveals that 60 copies of the monomer assemble into a thin, icosahedral shell with a diameter of 240 angstroms. The interior of this nanocompartment is lined with conserved binding sites for short polypeptide tags present as C-terminal extensions of enzymes involved in oxidative-stress response.

PubMed: 19172747
DOI: 10.1038/nsmb.1473

実験手法

X-RAY DIFFRACTION (3.104 Å)