Vladimir M. Korkhov

TL;DR: A general mass spectrometry approach is described to determine subunit stoichiometry and lipid binding in intact membrane protein complexes by subjecting the complex to multiple collisions and releasing the intact complex largely devoid of detergent.

TL;DR: The crystal structure of the transporter-binding protein complex BtuCD–BtuF trapped in an β-γ-imidoadenosine 5′-phosphate (AMP-PNP)-bound intermediate state is reported, suggesting an unexpected peristaltic transport mechanism that is distinct from those observed in other ABC transporters.

TL;DR: The structure suggests that monomeric TspO comprises five transmembrane α helices that form a homodimer, which is consistent with the dimeric state observed in detergent solution and indicates a possibility of two substrate translocation pathways per dimer.

TL;DR: It is shown that a motif in the COOH terminus of GAT1 (566RL567), which is conserved in SLC6 family members, is a binding site for the COPII coat component Sec24D, which provides a mechanistic explanation for the finding that oligomeric assembly of transporters is required for their ER export: transporter oligomerization supports efficient recruitment of COPII components.

TL;DR: The structure of the last missing state in the form of AMP-PNP–bound BtuCD, trapped by a disulfide cross-link is presented, thus rationalizing the roles of substrate, ATP and substrate-binding protein.