Search

Focal adhesion kinase (FAK) is a central mediator of cell adhesion, acting both as a scaffold and as catalytically active kinase. Acebrón et al (2020) use cryo-electron microscopy (cryo-EM) to visualize the dramatic structural changes that occur upon FAK recruitment to the plasma membrane, which releases FAK autoinhibition and induces its oligomerization. Since activity control via autoinhibition and protein clustering are features also utilized by other focal adhesion (FA) proteins, they have moved center stage in the endeavor to understand the complex process of cell adhesion regulation., (© 2020 The Authors.)

Copper (Cu+) transport ATPases are characterized by cytoplasmic metal-binding repeats. Using cryo-electron microscopy (cryo-EM) of functionally intact Cu+-ATPases and high-resolution structures of isolated domains, Wu et al. (2008) produced a model that explains how Cu+ binding to cytoplasmic sites controls the enzyme transport rate.

Tang et al. (2008) probe the virion structure of bacteriophage phi29 by asymmetric reconstructions of cryo-electron microscopy images, visualizing subunit conformations, protein-DNA interactions, and a novel twist of dsDNA that may aid in retention of the genome prior to ejection.

A high-resolution cryo-EM reconstruction of a ribosome-bound dicistrovirus IRES (Schüler et al., 2006) and the crystal structure of its ribosome binding domain (Pfingsten et al., 2006) provide new insights into an exceptional eukaryotic translation mechanism.

Structural information about the prokaryotic KirBac3.1 inward rectifier family K(+) channel from Magnetospirillum magnetotacticum is reported. These results from two-dimensional electron cryomicroscopy (EM) shed light on the gating mechanism of members of the Kir channel family.

The structure of a tetrameric form of the spider neurotoxin, alpha-latrotoxin, has been determined by single particle cryo-electron microscopy. It reveals a pore complex with extended arms that could bind receptors involved in synaptic vesicle exocytosis.