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  • 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

  • Cryo-EM Structure of a Human LECT2 Amyloid Fibril Reveals a Network of Polar Ladders at its Core

    • Authors : Richards, Logan S. (2023)

  • Amyloid diseases are linked to the formation and persistence of large, multimeric structures in various tissues. Amyloid fibrils are characterized by a cross-beta scaffold in which identical protein molecules mate tightly as beta-strands to form a long, unbranched fibril1,2. Before amyloid-forming proteins assemble into fibrils, they can display a globular fold, requiring partial or total unfolding to convert into an amyloid state3,4. Debilitating ne...
  • Journal article

  • Structure and function of a Notch-like proteolytic switch domain in the extracellular matrix receptor dystroglycan

    • Authors : Anderson, Michael J.M. (2023)

  • The adhesion receptor dystroglycan provides a critical mechanical link between the extracellular matrix (ECM) and the actin cytoskeleton to help muscle cells withstand contraction and neural cells maintain the blood brain barrier. Disrupting the link is associated cancer and muscular dystrophy. Proteolysis of dystroglycan by matrix metalloproteinases (MMPs) provides a mechanism to break the mechanical anchor and is amplified in several pathogenic states,&...
  • Journal Article

  • Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain

    • Authors : Jojoa-Cruz, Sebastian (2023)

  • Members of the OSCA/TMEM63 are mechanically activated ion channels and structures of some OSCA members have revealed the architecture of these channels and structural features that are potentially involved in mechanosensation. However, these structures are all in a similar state and information about the motion of different elements of the structure is limited, preventing a deeper understanding of how these channels work. Here, we use...
  • Journal Article

  • Structure of full-length cobalamin-dependent methionine synthase and cofactor loading captured in crystallo

    • Authors : Mendoza, Johnny (2023)

  • Cobalamin-dependent methionine synthase (MS) is a key enzyme in methionine and folate one-carbon metabolism. MS is a large multi-domain protein capable of binding and activating three substrates: homocysteine, folate, S-adenosylmethionine for methylation. Achieving three chemically distinct methylations necessitates significant domain rearrangements to facilitate substrate access to the cobalamin cofactor at the right time. The distinct conformations required for each r...