Abstract
Wiryaman & Toor [IUCrJ (2021). 8, 342-350] report the cryo-EM structure of a Thermotoga maritima encapsulin, a nanocompartment that encapsulates a ferritin-like protein cargo. The 2 Å resolution structure offers insights into the active role of this thermostable encapsulin in regulating iron homeostasis to reduce oxidative stress.
Highlights
In this issue of IUCrJ, Wiryaman and Toor at the University of California San Diego report the 2.0 Aresolution encapsulin structure of T. maritima (EncTm) using cryoelectron microscopy (cryo-EM) (Wiryaman & Toor, 2021)
In this issue of IUCrJ, Wiryaman and Toor at the University of California San Diego report the 2.0 Aresolution encapsulin structure of T. maritima (EncTm) using cryoelectron microscopy (Wiryaman & Toor, 2021). Their analysis identifies new structural features of EncTm related to major biological functions of encapsulins
The authors describe the structural basis of the high EncTm thermostability compared with mesophilic encapsulins, as well as a gating mechanism for iron ions in the very porous EncTm nanocompartment, and an unexpected flavin ligand on the outer surface of the protein shell that indicates an active role for EncTm in iron metabolism
Summary
In this issue of IUCrJ, Wiryaman and Toor at the University of California San Diego report the 2.0 Aresolution encapsulin structure of T. maritima (EncTm) using cryoelectron microscopy (cryo-EM) (Wiryaman & Toor, 2021). Their analysis identifies new structural features of EncTm related to major biological functions of encapsulins.
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