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Full-Text Articles in Life Sciences
Structural Insights Into The Architecture Of The Hyperthermophilic Fusellovirus Ssv1, Kenneth M. Stedman, Melissa Deyoung, Mitul Saha, Michael B. Sherman, Marc C. Morais
Structural Insights Into The Architecture Of The Hyperthermophilic Fusellovirus Ssv1, Kenneth M. Stedman, Melissa Deyoung, Mitul Saha, Michael B. Sherman, Marc C. Morais
Biology Faculty Publications and Presentations
The structure and assembly of many icosahedral and helical viruses are well-characterized. However, the molecular basis for the unique spindle-shaped morphology of many viruses that infect Archaea remains unknown. To understand the architecture and assembly of these viruses, the spindle-shaped virus SSV1 was examined using cryo-EM, providing the first 3D-structure of a spindle-shaped virus as well as insight into SSV1 biology, assembly and evolution. Furthermore, a geometric framework underlying the distinct spindle-shaped structure is proposed.
Novel Cul3 Binding Proteins Function To Remodel E3 Ligase Complexes, Wananit Wimuttisuk, Mark West, Brittney Davidge, Kebing Yu, Arthur Salomon, Jeffrey D. Singer
Novel Cul3 Binding Proteins Function To Remodel E3 Ligase Complexes, Wananit Wimuttisuk, Mark West, Brittney Davidge, Kebing Yu, Arthur Salomon, Jeffrey D. Singer
Biology Faculty Publications and Presentations
Background: Cullins belong to a family of scaffold proteins that assemble multi-subunit ubiquitin ligase complexes to recruit protein substrates for ubiquitination via unique sets of substrate adaptor, such as Skp1 or Elongin B, and a substrate-binding protein with a conserved protein-protein interacting domain, such as leucine-rich repeats (LRR), a WD40 domain, or a zinc-finger domain. In the case of the Cullin3 (Cul3), it forms a BTB-Cul3-Rbx1 (BCR) ubiquitin ligase complex where it is believed that a BTB domain-containing protein performs dual functions where it serves as both the substrate adaptor and …