Berlin-Karlsruhe - Macromolecular Crystallography BAG - Structural Biology of light responsive, signal transducing and metalloproteins

DOI

The project aims to investigate structure-function relationships in different groups of soluble and membrane proteins, most of which are involved in signal transduction or energy conversion. We investigate the signalling mechanisms of phytochromes by focusing on the structures of the intermediates of the photocycle and by analysing domain movements or by introducing unnatural amino acids. We analyse the structures of different G protein-coupled receptors (GPCRs; e.g. melanocortin-4 receptor and rhodopsin), either alone or in complex with their cognate G-proteins, to understand their signalling mechanisms. In our work on the biocatalytic splitting of molecular hydrogen into protons and electrons, we analyse the membrane-bound and soluble [NiFe] hydrogenases, proteins of the remarkably small subgroup of hydrogenases that are active under aerobic conditions. Other research areas include mechanosensitive channels, microbial rhodopsins, cytomegalovirus proteins and DNA photolyases.

Identifier
DOI https://doi.org/10.15151/ESRF-ES-1059388977
Metadata Access https://icatplus.esrf.fr/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatplus.esrf.fr:inv/1059388977
Provenance
Creator Luisa SAUTHOF; David FLOT ORCID logo; Binbin ZHOU; Manal EBRAHIM; Patrick SCHEERER ORCID logo
Publisher ESRF (European Synchrotron Radiation Facility)
Publication Year 2026
Rights CC-BY-4.0; https://creativecommons.org/licenses/by/4.0
OpenAccess true
Representation
Resource Type Data from large facility measurement; Collection
Discipline Particles, Nuclei and Fields