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  • Ebooks (Sách điện tử)

  • Structural insights into the initiation of free radical formation in the Class Ib ribonucleotide reductases

    • Authors : Yadav, Lumbini R. (2023)

  • Class I ribonucleotide reductases consisting of R1 and R2 subunits convert ribonucleoside diphosphates to deoxyribonucleoside diphosphates involving an intricate free radical mechanism. The generation of free radicals in the Class Ib ribonucleotide reductases is mediated by reaction involving di-manganese ions in the R2 subunits and is externally assisted by flavodoxin-like NrdI subunit. This is unlike Class Ia ribonucleotide reductases, where the free radical generation&#x...
  • Ebooks (Sách điện tử)

  • The structure of the neurotoxin palytoxin determined by MicroED

    • Authors : Gillman, Cody (2023)

  • Palytoxin (PTX) is a potent neurotoxin found in marine animals that can cause serious symptoms 17 such as muscle contractions, haemolysis of red blood cells and potassium leakage. Despite years 18 of research, very little is known about the mechanism of PTX. However, recent advances in the 19 field of cryoEM, specifically the use of microcrystal electron diffraction (MicroED), have allowed 20 us to determine the structure of PTX. It was&#x...
  • Journal article

  • Structure of a Membrane Tethering Complex Incorporating Multiple SNAREs

    • 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...
  • Journal article

  • Structural analysis of SALL4 zinc-finger domain reveals a link between AT-rich DNA binding and Okihiro syndrome

    • Authors : Watson, James A. (2023)

  • Spalt-like 4 (SALL4) maintains vertebrate embryonic stem cell identity and is required for the development of multiple organs, including limbs. Mutations in SALL4 are associated with Okihiro syndrome and SALL4 is also a known target of thalidomide. SALL4 protein has a distinct preference for AT-rich sequences, recognised by a pair of zinc fingers at the C-terminus. However, unlike many characterised zinc finger proteins, SALL4 shows flexibl...
  • Journal article

  • An alphacoronavirus polymerase structure reveals conserved co-factor functions

    • 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...
  • Journal article

  • Structure of the human Bre1 complex bound to the nucleosome

    • Authors : Onishi, Shuhei  (2023)

  • Histone H2B monoubiquitination (at Lys120 in humans) regulates transcription elongation and DNA repair. In humans, H2B monoubiquitination is catalyzed by the heterodimeric Bre1 complex composed of Bre1A/RNF20 and Bre1B/RNF40. The Bre1 proteins generally function as tumor suppressors, while in certain cancers, they facilitate cancer cell proliferation. To reveal the structural basis of H2BK120 ubiquitination and its regulation, we determined the cryo-EM structure of...
  • Journal article

  • CryoEM Structures of the Nitrogenase Complex During Catalytic Turnover

    • 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 ...