@article{8581,
  abstract     = {The majority of adenosine triphosphate (ATP) powering cellular processes in eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo, determined by cryo-electron microscopy. Subunits in the membrane domain are arranged in the ‘proton translocation cluster’ attached to the c-ring and a more distant ‘hook apparatus’ holding subunit e. Unexpectedly, this subunit is anchored to a lipid ‘plug’ capping the c-ring. We present a detailed proton translocation pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled c-ring, suggesting permeability transition pore opening. We propose a model for the permeability transition pore opening, whereby subunit e pulls the lipid plug out of the c-ring. Our structure will allow the design of drugs for many emerging applications in medicine.},
  author       = {Pinke, Gergely and Zhou, Long and Sazanov, Leonid A},
  issn         = {15459985},
  journal      = {Nature Structural and Molecular Biology},
  number       = {11},
  pages        = {1077--1085},
  publisher    = {Springer Nature},
  title        = {{Cryo-EM structure of the entire mammalian F-type ATP synthase}},
  doi          = {10.1038/s41594-020-0503-8},
  volume       = {27},
  year         = {2020},
}

@article{515,
  abstract     = {The oxidative phosphorylation electron transport chain (OXPHOS-ETC) of the inner mitochondrial membrane is composed of five large protein complexes, named CI-CV. These complexes convert energy from the food we eat into ATP, a small molecule used to power a multitude of essential reactions throughout the cell. OXPHOS-ETC complexes are organized into supercomplexes (SCs) of defined stoichiometry: CI forms a supercomplex with CIII2 and CIV (SC I+III2+IV, known as the respirasome), as well as with CIII2 alone (SC I+III2). CIII2 forms a supercomplex with CIV (SC III2+IV) and CV forms dimers (CV2). Recent cryo-EM studies have revealed the structures of SC I+III2+IV and SC I+III2. Furthermore, recent work has shed light on the assembly and function of the SCs. Here we review and compare these recent studies and discuss how they have advanced our understanding of mitochondrial electron transport.},
  author       = {Letts, James A and Sazanov, Leonid A},
  issn         = {15459993},
  journal      = {Nature Structural and Molecular Biology},
  number       = {10},
  pages        = {800 -- 808},
  publisher    = {Nature Publishing Group},
  title        = {{Clarifying the supercomplex: The higher-order organization of the mitochondrial electron transport chain}},
  doi          = {10.1038/nsmb.3460},
  volume       = {24},
  year         = {2017},
}

@article{603,
  abstract     = {During transcription, RNA polymerase II (Pol II) associates with the conserved elongation factor DSIF. DSIF renders the elongation complex stable and functions during Pol II pausing and RNA processing. We combined cryo-EM and X-ray crystallography to determine the structure of the mammalian Pol II-DSIF elongation complex at a nominal resolution of 3.4. Human DSIF has a modular structure with two domains forming a DNA clamp, two domains forming an RNA clamp, and one domain buttressing the RNA clamp. The clamps maintain the transcription bubble, position upstream DNA, and retain the RNA transcript in the exit tunnel. The mobile C-terminal region of DSIF is located near exiting RNA, where it can recruit factors for RNA processing. The structure provides insight into the roles of DSIF during mRNA synthesis.},
  author       = {Bernecky, Carrie A and Plitzko, Jürgen and Cramer, Patrick},
  issn         = {15459993},
  journal      = {Nature Structural and Molecular Biology},
  number       = {10},
  pages        = {809 -- 815},
  publisher    = {Nature Publishing Group},
  title        = {{Structure of a transcribing RNA polymerase II-DSIF complex reveals a multidentate DNA-RNA clamp}},
  doi          = {10.1038/nsmb.3465},
  volume       = {24},
  year         = {2017},
}