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The major photosynthetic apparatus of purple phototrophic bacteria comprises two distinct complexes: the light-harvesting (LH) complex and the reaction center (RC). Here, the authors report a cryo-EM structure of a distinct conjoined LH1–LH2 complex from extremophile Hlr. halophila.

Rhodobacter sphaeroides is a model organism for studying bacterial photosynthesis. Here, the authors present structures of its native dimeric and a protein-U-lacking monomeric light-harvesting-reaction center complexes, which reveal asymmetric features for the dimer and an altered shape for the monomer.

Here the authors report a cryo-EM structure of the light-harvesting-reaction center complex (LH1- RC) from the purple phototrophic bacterium Thiorhodovibrio strain 970, providing insights into the mechanisms that underlie the absorbance properties of both the LH1 and the RC of this spectrally unusual purple bacterium.

Tani et al. present the cryo-EM structure of the endothelin type B receptor (ETBR) in complex with the Gi protein, emphasizing the movements of transmembrane helix 7 during ETBR activation. The study underscores the crucial role of the NPxxL motif in stabilizing the receptor's active state and organizing the Gi protein binding site, enhancing our understanding of GPCR activation and aiding therapeutic development.

Rhodobacter capsulatus is a favored model organism for studying bacterial photosynthesis. Here the authors present a structure of its light-harvesting–reaction center complex, which reveals that it forms a crescent shape containing only 10 LH1 αβ-subunits.

Rhodobacter (Rba.) sphaeroides is a model organism for studying bacterial photosynthesis. Here, the authors present the 2.9 Å cryo-EM structure of the monomeric light-harvesting-reaction center core complex from Rba. sphaeroides strain IL106, which revealed the position and conformation of PufX and the presence of an additional component protein-U, an integral membrane protein.

The bacterial light-harvesting–reaction center in complex with its electron donor HiPIP in their native form is presented, characterized and discussed with mechanistic implications for the photosynthetic electron transfer pathway.

The cryo-EM structure of the partially Ca^2 + -bound light-harvesting 1–reaction center (LH1–RC) complex from Alc. vinosum, the best-studied model purple sulfur bacterium, is presented, characterized and compared to other photosynthetic bacteria.

The cryo-EM structure of the unusual light-harvesting 1–reaction center (LH1–RC) complex from Rpi. globiformis, the most acidophilic anaerobic purple bacteria, is presented, characterized and compared to other photosynthetic bacteria.

Gap junctions have critical roles in maintaining homeostasis in multicellular organisms. Here the authors present cryo-EM structures of the C. elegansinnexin-6 gap junction channel, revealing high structural similarity to human connexin 26 despite a different oligomeric number and lack of sequence similarity.

IP39 is an abundant protozoan protein known to form highly-ordered striations in Euglena gracilis’ plasma membrane. Here, Suzuki et al. determine its three-dimensional structure by electron crystallography revealing that IP39 polymerises to form trimeric longitudinal units arranged in a molecular strand of antiparallel double-rows.

The gastric proton pump, H⁺,K⁺-ATPase, contributes to stomach acidification and is a target of acid suppressants. Here, the three-dimensional structure of the pump is determined using electron crystallography, providing the first structural information about the binding of a new class of acid suppressants.

The X-ray crystal structures of human endothelin type B receptor in the ligand-free form and in complex with the endogenous agonist endothelin-1.

Crystal structures of human endothelin ET_B receptor bound to bosentan and to ET_B-selective derivative provide insight into the basis of antagonism by these drugs.