Nature Search

A short intrinsically disordered region at KtrB’s N-terminus facilitates allosteric regulation of K⁺ channel KtrAB

KtrAB is a major potassium uptake system that has been linked to the pathogenesis of many infectious bacteria. Here the authors show that KtrB from Vibrio alginolyticus contains an intrinsically disordered N-terminus that is key to its regulation.

Janina Stautz
David Griwatz
Inga Hänelt
ResearchOpen Access07 May 2025
Nature Communications

Volume: 16, P: 1-16
Conformational coupling of redox-driven Na⁺-translocation in Vibrio cholerae NADH:quinone oxidoreductase

By obtaining structural snapshots of the catalytic cycle of NADH:quinone oxidoreductase from Vibrio cholerae, the authors uncover its mechanism. They show how electrons are shuttled and determine the importance of the [2Fe-2S] cluster in the movement of the electron transfer switch.

Jann-Louis Hau
Susann Kaltwasser
Günter Fritz
ResearchOpen Access14 Sept 2023
Nature Structural & Molecular Biology

Volume: 30, P: 1686-1694
Cyclic di-AMP traps proton-coupled K⁺ transporters of the KUP family in an inward-occluded conformation

Second messengers regulate a broad spectrum of processes in bacteria. Here, authors characterize how the second messenger cyclic di-AMP inhibits the potassium transporter KimA using cryo-EM, molecular dynamics simulations and functional assays.

Michael F. Fuss
Jan-Philip Wieferig
Inga Hänelt
ResearchOpen Access21 Jun 2023
Nature Communications

Volume: 14, P: 1-12
Structural basis of proton-coupled potassium transport in the KUP family

KUP transporters facilitate potassium uptake by the co-transport of protons and are key players in potassium homeostasis. Here authors identify the potassium importer KimA from Bacillus subtilis as a new member of the KUP transporter family and show the cryo-EM structure of KimA in an inward-occluded, trans-inhibited conformation.

Igor Tascón
Joana S. Sousa
Inga Hänelt
ResearchOpen Access31 Jan 2020
Nature Communications

Volume: 11, P: 1-10
Structural basis for energy transduction by respiratory alternative complex III

Some prokaryotes use alternative respiratory chain complexes, such as the alternative complex III (ACIII), to generate energy. Here authors provide the cryoEM structure of ACIII from Rhodothermus marinus which shows the arrangement of cofactors and provides insights into the mechanism for energy transduction.

Joana S. Sousa
Filipa Calisto
Manuela M. Pereira
ResearchOpen Access30 Apr 2018
Nature Communications

Volume: 9, P: 1-10
Respiratory supercomplexes III₂IV₂ come into focus

Structural information on the respiratory supercomplex III₂IV₂ from budding yeast and from Mycobacterium smegmatis has become available, with cryo-EM work from four different groups.

Joana S. Sousa
Janet Vonck
News & Views28 Jan 2019
Nature Structural & Molecular Biology

Volume: 26, P: 87-89
Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase

Electron cryomicroscopy of a complete mitochondrial ATP-synthase dimer reveals the elusive structure of the essential a-subunit.

Matteo Allegretti
Niklas Klusch
Karen M. Davies
Research23 Feb 2015
Nature

Volume: 521, P: 237-240
Analysis of the co-translational assembly of the fungal fatty acid synthase (FAS)

Manuel Fischer
Mirko Joppe
Martin Grininger
ResearchOpen Access21 Jan 2020
Scientific Reports

Volume: 10, P: 1-13

Search

A short intrinsically disordered region at KtrB’s N-terminus facilitates allosteric regulation of K⁺ channel KtrAB

Conformational coupling of redox-driven Na⁺-translocation in Vibrio cholerae NADH:quinone oxidoreductase

Cyclic di-AMP traps proton-coupled K⁺ transporters of the KUP family in an inward-occluded conformation

Structural basis of proton-coupled potassium transport in the KUP family

Structural basis for energy transduction by respiratory alternative complex III

Respiratory supercomplexes III₂IV₂ come into focus

Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase

Analysis of the co-translational assembly of the fungal fatty acid synthase (FAS)

Search

Quick links

Search

Filter By:

Search

Quick links