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Showing results 1 to 12 of 12
  • OER000002580.pdf.jpg
  • Journal article


  • Authors : Anderson, Thomas K. (2023)

  • Coronaviruses are a diverse subfamily of viruses containing pathogens of humans and animals. This subfamily of viruses replicates their RNA genomes using a core polymerase complex composed of viral non-structural proteins: nsp7, nsp8 and nsp12. Most of our understanding of coronavirus molecular biology comes from the betacoronaviruses like SARS-CoV and SARSCoV- 2, the latter of which is the causative agent of COVID-19. In...

  • OER000002697.pdf.jpg
  • Journal article


  • Authors : Rutledge, Hannah L. (2023)

  • The enzyme nitrogenase couples adenosine triphosphate (ATP) hydrolysis to the multi-electron reduction of atmospheric dinitrogen into ammonia. Despite extensive research, the mechanistic details of ATP-dependent energy transduction and dinitrogen reduction by nitrogenase are not well understood, requiring new strategies to monitor its structural dynamics during catalytic action. Here we report the cryogenic electron microscopic interrogation of the nitrogenase complex under enzymatic ...

  • OER000002449.pdf.jpg
  • Ebooks (Sách điện tử)


  • Authors : Blikstad, Cecilia (2023)

  • Carboxysomes are proteinaceous organelles that encapsulate key enzymes of CO2 fixation - Rubisco and carbonic anhydrase - and are the centerpiece of the bacterial CO2 concentrating mechanism (CCM). In the CCM, actively accumulated cytosolic bicarbonate diffuses into the carboxysome and is converted to CO2 by carbonic anhydrase, producing a high CO2 concentration near Rubisco and ensuring efficient carboxylation. Self-assembly of the α-carboxysome is...

  • OER000002607.pdf.jpg
  • Journal article


  • Authors : Kustusz, Agata Gluszek (2023)

  • During mitosis, spindle architecture alters as chromosomes segregate to daughter cells. The microtubule crosslinker Protein Required for Cytokinesis 1 (PRC1) is essential for spindle stability, chromosome segregation and completion of cytokinesis, but how it recruits motors to the central spindle to coordinate the segregation of chromosomes is unknown. Here, we combine structural and cell biology approaches to show that the human CENP-E motor, which&...

  • OER000003013.pdf.jpg
  • Journal article


  • Authors : Weekley, Claire M. (2021)

  • Since SARS-CoV-2 emerged in 2019, genomic sequencing has identified mutations in the viral RNA including in the receptor-binding domain of the Spike protein. Structural characterisation of the Spike carrying point mutations aids in our understanding of how these mutations impact binding of the protein to its human receptor, ACE2, and to therapeutic antibodies. The Spike G485R mutation has been observed in multiple isolates of the virus and mutation ...

  • OER000002309.pdf.jpg
  • Journal Article


  • Authors : Bryan, Nikaela W. (2023)

  • Membraneless intracellular compartmentalization is central to a long and growing list of biochemical transactions at diverse sub-cellular locations 1. Proteins are by-and-large the drivers of the formation of these compartments, but there is debate about whether their underpinnings are either low-affinity/low-specificity interactions yielding phase separation 2 or multivalent site-specific interactions 3. By its very nature, ascertaining the former type of &#x...

  • OER000002677.pdf.jpg
  • Journal article


  • Authors : Boom, Johannes van den (2023)

  • The AAA+ ATPase p97 (also called VCP, or Cdc48 in yeast) unfolds proteins and disassembles protein complexes in a myriad of cellular processes, but how a substrate complex needs to be loaded onto p97 by a dedicated substrate adapter and then disassembled by p97 has not been structurally visualized so far. Here we present cryo-EM structures of p97 in the process of disassembling a protein phosphatase-1 (PP1) complex by &#...

  • OER000002498.pdf.jpg
  • Journal article


  • Authors : Schmidt, Frederik V.  (2023)

  • Nitrogenases are best known for catalysing the reduction of dinitrogen to ammonia at a complex metallic cofactor. Recently, nitrogenases were shown to reduce carbon dioxide (CO2) and carbon monoxide to hydrocarbons, offering a pathway to recycle carbon waste into hydrocarbon products. Among the nitrogenase family the iron nitrogenase is the isozyme with the highest wildtype activity for the reduction of CO2, but the molecular architecture facilitating these&#...

  • OER000002499.pdf.jpg
  • Journal article


  • Authors : Panigrahi, Rashmi  (2023)

  • MDC1 is a key mediator of DNA-damage signaling. When DNA double-strand breaks (DSB) occur, the histone variant H2AX on the nucleosome is phosphorylated on its C-terminus at residue Ser139 to form the γH2AX nucleosome. This phosphorylated form is specifically recognized by the tandem BRCT repeats of MDC1. The MDC1-bound nucleosome serves as a docking platform to promote the localization of other DNA repair factors. To further characteri...

  • OER000002295.pdf.jpg
  • Journal Article


  • Authors : Ikei, Mai (2023)

  • From bacteria to eukaryotes, sulfur is a vital element for cellular activities. For example, sulfur34 containing biomolecules, such as L-cysteine, L-methionine, thiamine, glutathione, and biotin, play a 35 variety of essential roles in cells (1). Bacteria and plants can utilize L-cysteine as a source of sulfate, 36 but they also have sulfur assimilation pathways to synthesize L-cysteine from inorganic sulfur 37 compounds. In bacteria, L-cysteine...

  • OER000002656.pdf.jpg
  • Journal article


  • Authors : DAmico, Kevin A. (2023)

  • Most membrane fusion reactions in eukaryotic cells are mediated by membrane tethering 17 complexes (MTCs) and SNARE proteins. MTCs are much larger than SNAREs and are thought 18 to mediate the initial attachment of two membranes. Complementary SNAREs then form 19 membrane-bridging complexes whose assembly draws the membranes together for fusion. Here, 20 we present a cryo-EM structure of the simplest known MTC, the 255-kDa Dsl1 complex...

  • OER000002977.pdf.jpg
  • Journal article


  • Authors : Kolata, Piotr (2021)

  • Respiratory complex I is a multi-subunit membrane protein complex that reversibly couples NADH oxidation and ubiquinone reduction with proton translocation against trans-membrane potential. Complex I from Escherichia coli is among the best functionally characterizedcomplexes, but its structure remains unknown, hindering further mechanistic studies to understand the enzyme coupling mechanism. Here we describe the single particle cryo electron microscopy (cryo-EM) structure of th...