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Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA

Elevator transporters, like SLC23 proteins, transport solutes by a mechanism involving a reorientation of two rigid domains. Here, the authors show that linkers connecting these domains control the carrier’s conformational space and thus its function.

Benedikt T. Kuhn
Jonathan Zöller
Eric R. Geertsma
ResearchOpen Access30 Aug 2024
Nature Communications

Volume: 15, P: 1-12
Correction: Corrigendum: Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family

Eric R Geertsma
Yung-Ning Chang
Raimund Dutzler
Amendments and Corrections04 May 2016
Nature Structural & Molecular Biology

Volume: 23, P: 462
Structural basis for functional interactions in dimers of SLC26 transporters

The SLC26 family of transporters maintains anion equilibria in all kingdoms of life. Here, the authors resolve the structure of an SLC26 dimer embedded in a lipid membrane and characterize it by PELDOR/DEER distance measurements, biochemical studies with MD simulations and spin-label ensemble refinement.

Yung-Ning Chang
Eva A. Jaumann
Eric R. Geertsma
ResearchOpen Access02 May 2019
Nature Communications

Volume: 10, P: 1-10
Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family

SLC26 membrane proteins constitute a large family of anion transporters with diverse functions. The first structure of a full-length SLC26 transporter now provides a common framework for the architecture of this protein family.

Eric R Geertsma
Yung-Ning Chang
Raimund Dutzler
Research14 Sept 2015
Nature Structural & Molecular Biology

Volume: 22, P: 803-808
High-throughput cloning and expression in recalcitrant bacteria

Eric R Geertsma
Bert Poolman
Research22 Jul 2007
Nature Methods

Volume: 4, P: 705-707
Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport

The X-ray crystal structure of ScaDMT, a bacterial member of the solute carrier 11 transporter family, identifies conserved residues within the substrate-binding site that confer metal-ion selectivity.

Ines A Ehrnstorfer
Eric R Geertsma
Raimund Dutzler
Research19 Oct 2014
Nature Structural & Molecular Biology

Volume: 21, P: 990-996
Generation of synthetic nanobodies against delicate proteins

This protocol describes in vitro procedures for generation of synthetic single-domain antibodies called ‘sybodies’. Sybodies can be engineered to target specific protein conformations, labile membrane proteins or protein complexes.

Iwan Zimmermann
Pascal Egloff
Markus A. Seeger
Protocols08 Apr 2020
Nature Protocols

Volume: 15, P: 1707-1741
Conformation space of a heterodimeric ABC exporter under turnover conditions

Eight cryo-electron microscopy structures of the ATP-binding cassette exporter TmrAB under turnover conditions characterize the entire transport cycle in a lipid environment.

Susanne Hofmann
Dovile Januliene
Arne Moeller
Research17 Jul 2019
Nature

Volume: 571, P: 580-583
Genetic and pharmacological reduction of CDK14 mitigates synucleinopathy

Jean-Louis A. Parmasad
Konrad M. Ricke
Maxime W. C. Rousseaux
ResearchOpen Access04 Apr 2024
Cell Death & Disease

Volume: 15, P: 1-13
Selection of nanobodies with broad neutralizing potential against primary HIV-1 strains using soluble subtype C gp140 envelope trimers

Kathrin Koch
Sarah Kalusche
Ursula Dietrich
ResearchOpen Access21 Aug 2017
Scientific Reports

Volume: 7, P: 1-15
Membrane reconstitution of ABC transporters and assays of translocator function

Eric R Geertsma
N A B Nik Mahmood
Bert Poolman
Protocols31 Jan 2008
Nature Protocols

Volume: 3, P: 256-266

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