Min Zhou

TL;DR: It is shown that rotary adenosine triphosphatases (ATPases)/synthases from Thermus thermophilus and Enterococcus hirae can be maintained intact with membrane and soluble subunit interactions preserved in vacuum and can link specific lipid and nucleotide binding with distinct regulatory roles.

TL;DR: A detailed investigation of the composition and structure of the CSM complex from the archaeon Sulfolobus solfataricus is reported, using a combination of electron microscopy, mass spectrometry, and deep sequencing that reveals a three-dimensional model that includes a helical component strikingly reminiscent of the backboneructure of the type I (Cascade) family.

TL;DR: This review highlights recent insights gained, surveys methods being developed for probing protein-lipid interactions, and focuses specifically on the potential of mass spectrometry in this growing area of research.

TL;DR: Conformational changes at the catalytic interface, evidenced by changes in cross-linking, provide a rationale for reduced nucleotide occupancy and highlight a role for phosphorylation in regulating nucleotide binding and stability of the chloroplast ATPase.

TL;DR: Differences that can be related to conformational changes in the Vo complex triggered by ATP binding are revealed by isolating complexes at different phases of cell growth and manipulating nucleotides, metal ions and pH during isolation.