Browse our latest Structural Biology and Molecular Biophysics articles

As the function of membrane proteins is often influenced by its membrane environment the presented combinatorial approach is of great value for the investigation of membrane protein complexes in natural or even manipulated lipid bilayers.

The structural and functional analysis of the ATP-dependent RNA helicase Prp43 provides insights into the mechanisms of RNA binding and translocation, which could serve as paradigm for all DEAH-box proteins.

Solid state NMR is unable to detect any association of substrate to the second binding site, S2, in the extracellular vestibule of the Neurotransmitter:Sodium Symporter LeuT.

The centromeric protein CENP-T assembles the microtubule-binding interface of kinetochores through direct recruitment of two Ndc80 complexes and indirect recruitment of a third one through the Mis12 complex.

DNA-bound crystal structures of an essential Xer site-specific recombinase from the bacterium Helicobacter pylori reveal how large conformational changes initiate the untangling of chromosomes upon cell division.

Building on previous work (Chatterjee et al., 2014), the mechanism of coincidence detection in bacterial second messenger signaling across membranes is revealed at a molecular level, providing insight into the regulation of a conserved transmembrane receptor.

The molecular mechanism of switching between phosphotransferase- and phosphatase-competent states in histidine-kinases has been uncovered, through direct crystallographic observation of bona fide complexes between a histidine-kinase and its response regulator from Bacillus subtilise.

Mice deficient in the TRPM6 channel suffer from impaired prenatal development, shortened lifespan, growth deficit and disturbed energy balance due to a defect in epithelial Mg²⁺ uptake, thus highlighting a pivotal role of TRPM6 in organismal Mg²⁺ homeostasis.

Building on previous work (Wilkinson et al, 2016), it is shown that inhibition of RecBCD-induced DNA break repair can be used as a co-antibacterial strategy with quinolones.

Biochemical and structural analyses of a universal mRNP remodeling pathway suggest an ATPase-powered targeted deposition of export factors onto mRNP.