-
Article
Open AccessAuthor Correction: Determining protein structures in cellular lamella at pseudo-atomic resolution by GisSPA
-
Article
Open AccessThe structural basis for light acclimation in phycobilisome light harvesting systems systems in Porphyridium purpureum
Photosynthetic organisms adapt to changing light conditions by manipulating their light harvesting complexes. Biophysical, biochemical, physiological and genetic aspects of these processes are studied extensiv...
-
Article
Nuclear export of pre-60S particles through the nuclear pore complex
The nuclear pore complex (NPC) is the bidirectional gate that mediates the exchange of macromolecules or their assemblies between nucleus and cytoplasm1–3. The assembly intermediates of the ribosomal subunits, pr...
-
Article
In situ structure of the red algal phycobilisome–PSII–PSI–LHC megacomplex
In oxygenic photosynthetic organisms, light energy is captured by antenna systems and transferred to photosystem II (PSII) and photosystem I (PSI) to drive photosynthesis1,2. The antenna systems of red algae cons...
-
Article
Open AccessDetermining protein structures in cellular lamella at pseudo-atomic resolution by GisSPA
Cryo-electron tomography is a major tool used to study the structure of protein complexes in situ. However, the throughput of tilt-series image data collection is still quite low. Here, we show that GisSPA, a ...
-
Article
Open AccessStructure of the Acidobacteria homodimeric reaction center bound with cytochrome c
Photosynthesis converts light energy to chemical energy to fuel life on earth. Light energy is harvested by antenna pigments and transferred to reaction centers (RCs) to drive the electron transfer (ET) reacti...
-
Article
Open AccessStructural insights into PA3488-mediated inactivation of Pseudomonas aeruginosa PldA
PldA, a phospholipase D (PLD) effector, catalyzes hydrolysis of the phosphodiester bonds of glycerophospholipids—the main component of cell membranes—and assists the invasion of the opportunistic pathogen Pseudom...
-
Article
Open AccessNear-atomic structure of the inner ring of the Saccharomyces cerevisiae nuclear pore complex
Nuclear pore complexes (NPCs) mediate bidirectional nucleocytoplasmic transport of substances in eukaryotic cells. However, the accurate molecular arrangement of NPCs remains enigmatic owing to their huge size...
-
Article
Structural insights into cyanobacterial photosystem II intermediates associated with Psb28 and Tsl0063
Photosystem II (PSII) is a multisubunit pigment–protein complex and catalyses light-induced water oxidation, leading to the conversion of light energy into chemical energy and the release of dioxygen. We analy...
-
Article
Open AccessAntenna arrangement and energy-transfer pathways of PSI–LHCI from the moss Physcomitrella patens
Plants harvest light energy utilized for photosynthesis by light-harvesting complex I and II (LHCI and LHCII) surrounding photosystem I and II (PSI and PSII), respectively. During the evolution of green plants...
-
Article
Open AccessStructural basis for energy transfer in a huge diatom PSI-FCPI supercomplex
Diatom is an important group of marine algae and contributes to around 20% of the global photosynthetic carbon fixation. Photosystem I (PSI) of diatoms is associated with a large number of fucoxanthin-chloroph...
-
Article
Structural basis of energy transfer in Porphyridium purpureum phycobilisome
Photosynthetic organisms have developed various light-harvesting systems to adapt to their environments1. Phycobilisomes are large light-harvesting protein complexes found in cyanobacteria and red algae2–4, altho...
-
Article
Structure of a green algal photosystem I in complex with a large number of light-harvesting complex I subunits
Photosystem I (PSI) is a highly efficient natural light-energy converter, and has diverse light-harvesting antennas associated with its core in different photosynthetic organisms. In green algae, an extremely ...
-
Article
Open AccessStructural basis for specific flagellin recognition by the NLR protein NAIP5
The nucleotide-binding domain- and leucine-rich repeat (LRR)-containing proteins (NLRs) function as intracellular immune receptors to detect the presence of pathogen- or host-derived signals. The mechanisms of...
-
Article
Structure of phycobilisome from the red alga Griffithsia pacifica
Life on Earth depends on photosynthesis for its conversion of solar energy to chemical energy. Photosynthetic organisms have developed a variety of light-harvesting systems to capture sunlight. The largest lig...
-
Article
Open AccessCryo-EM structures of the ATP-bound Vps4E233Q hexamer and its complex with Vta1 at near-atomic resolution
The cellular ESCRT-III (endosomal sorting complex required for transport-III) and Vps4 (vacuolar protein sorting 4) comprise a common machinery that mediates a variety of membrane remodelling events. Vps4 is e...
-
Article
Cryo-EM structure of Nma111p, a unique HtrA protease composed of two protease domains and four PDZ domains
-
Article
Structural organization of an intact phycobilisome and its association with photosystem II
Phycobilisomes (PBSs) are light-harvesting antennae that transfer energy to photosynthetic reaction centers in cyanobacteria and red algae. PBSs are supermolecular complexes composed of phycobiliproteins (PBPs...
-
Article
Cryo-EM structure of SNAP-SNARE assembly in 20S particle
N-ethylmaleimide-sensitive factor (NSF) and α soluble NSF attachment proteins (α-SNAPs) work together within a 20S particle to disassemble and recycle the SNAP receptor (SNARE) complex after intracellular memb...
-
Article
Structural characterization of full-length NSF and 20S particles
The 20S particle, which is composed of NSF, SNAP and the SNARE complex, is important in fusion events. Single-particle cryo-EM and negative stain EM studies of the 20S particle and of NSF in its different nucl...