Structural biology articles from across Nature Portfolio

Structural flexibility is often considered a challenge in protein design, but it brings opportunities for creating protein assemblies that have several defined structures. A study now suggests that the controllable design of oligomorphic protein assemblies could be achieved by modulating structural flexibility.

NMR spectroscopy is a critical tool for linking protein structure, dynamics and interactions to protein function, but is challenging to apply to high-molecular-weight proteins. The chemical synthesis of an NMR probe combines the advantages of four different nuclei, ¹H, ²H, ¹³C and ¹⁹F, to achieve optimal resolution for these larger systems.

The lysosomal transmembrane protein LYCHOS enables activation of the master growth regulator mTORC1 kinase by cholesterol. Here we summarize recent structural findings that shed light on the LYCHOS cholesterol-binding site and its role in mTORC1 activation.

Here, the authors present the crystal structure of Transportin 3 (TNPO3) bound to its cargo cold-inducible RNA-binding protein (CIRBP), uncovering a distinct mechanism of protein nuclear import regulation independent of phosphorylation.

Nitrogen-oxygen-sulfur (NOS) linkages serve as crucial allosteric redox switches in proteins, yet their diversity beyond lysine-cysteine pairs remains underexplored. Here, the authors employ machine learning and quantum-mechanical calculations to identify 69 NOS bonds, expanding protein chemistry’s landscape and offering new avenues for drug design and protein engineering.

The association and dissociation dynamics of the ECF transporter complex for vitamin B12 are visualized by single-molecule FRET, highlighting the original transport mechanism of this group of ABC transporters.

In this Review we discuss the fascinating molecular details of the small molecules and peptides promoting plant protein–protein interactions, and their relevance for plant development and environmental responses.

Structural flexibility is often considered a challenge in protein design, but it brings opportunities for creating protein assemblies that have several defined structures. A study now suggests that the controllable design of oligomorphic protein assemblies could be achieved by modulating structural flexibility.

NMR spectroscopy is a critical tool for linking protein structure, dynamics and interactions to protein function, but is challenging to apply to high-molecular-weight proteins. The chemical synthesis of an NMR probe combines the advantages of four different nuclei, ¹H, ²H, ¹³C and ¹⁹F, to achieve optimal resolution for these larger systems.

The lysosomal transmembrane protein LYCHOS enables activation of the master growth regulator mTORC1 kinase by cholesterol. Here we summarize recent structural findings that shed light on the LYCHOS cholesterol-binding site and its role in mTORC1 activation.

The high-resolution structure of a bridge-like lipid-transfer protein that moves lipids between cellular compartments shows how these ‘lipid superhighways’ operate.