Browse our latest Structural Biology and Molecular Biophysics articles

X-ray crystallography reveals that the Dna2 nuclease-helicase contains a long tunnel through which single-stranded DNA threads, and an allosteric mechanism for displacing the DNA-binding protein Rpa that restricts cleavage to the proper polarity.

The ciliary G-protein Arl13B – which is often mutated in Joubert syndrome – is the Guanine nucleotide exchange factor for the G-protein Arl3 and exclusively localizes to cilia.

The conformations of the enzyme cyclophilin A that are essential for its catalytic activity are temperature dependent and exhibit diverse responses, which is consistent with a complex energy landscape.

The subunits of the SpoIIIE motor contact the 5'→3' strand of DNA in sequence to rapidly translocate the DNA across a membrane.

Nascent regulatory peptides tune the translation rate through a continuous, dynamic reshaping of the functional center of the ribosome.

Compressive force spectroscopy of single molecules reveals that intra-protein forces underlie the long-distance coordination of structural changes within a cytotoxin during pore formation.

A buried mutation in αβ-tubulin reveals an allosteric response to GDP in the lattice that dictates microtubule catastrophe and shrinking.

Structures of the replicative DNA polymerase Pol IIIα, the DNA sliding clamp, the proofreading exonuclease, and the processivity switch Tau (τ) suggest a mechanism for quick release during lagging strand synthesis.

Structural analysis of the ATP synthase – in combination with evolutionary covariance analysis – reveals the fold of the a subunit and shows that the enzyme can adopt several different conformations, which support the Brownian ratchet model for generating rotation.