I. Gutsche

Structural landscape of the Respiratory Syncytial Virus nucleocapsids

This paper presents cryo-EM structures of RSV nucleocapsids, revealing their polymorphism and unique helical symmetry due to C-terminal N interactions.

The AAA+ ATPase RavA and its binding partner ViaA modulate E. coli aminoglycoside sensitivity through interaction with the inner membrane

This study identifies RavA and ViaA as modulators of E. coli aminoglycoside sensitivity through lipid interactions affecting membrane morphology and antibiotic resistance.

Characterization of the interaction domains between the phosphoprotein and the nucleocapsid of human Metapneumovirus

This paper identifies the specific domains of the HMPV phosphoprotein (P) and nucleocapsid (NNuc) that mediate their interaction, showing the C-terminal 6 residues of P and the N-terminal domain of N are critical.

Alternative architecture of the E. coli chemosensory array

The paper presents cryo-electron tomography images of E. coli chemosensory arrays showing a p2-symmetric architecture, differing from the previously described p6-symmetric structure, and proposes molecular models for both.

Tools enabling flexible approaches to high-resolution subtomogram averaging

The paper introduces computational tools for subtomogram averaging in cryo-electron tomography, demonstrating their application to HIV-1 and bacterial datasets.

Complete structure of the core signalling unit of the E. coli chemosensory array in an optimised minicell strain

The paper presents a 3D map of the E. coli chemosensory core signalling unit using cryo-ET and subtomogram averaging, combined with molecular dynamics simulations to create an atomistic model.

Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors

The paper investigates how bortezomib activates ClpP protease by mimicking a substrate and inducing allosteric conformational changes that enhance its interaction with ClpX.

Identification of a novel subfamily of bacterial AAT-fold basic amino acid decarboxylases and functional characterization of its first representative: Pseudomonas aeruginosa LdcA

The paper identifies a novel subfamily of bacterial AAT-fold lysine decarboxylases, LdcA, and characterizes its role in Pseudomonas aeruginosa polyamine production and drug resistance.