Curvature of the Retroviral Capsid Assembly Is Modulated by a Molecular Switch

التفاصيل البيبلوغرافية
العنوان: Curvature of the Retroviral Capsid Assembly Is Modulated by a Molecular Switch
المؤلفون: Tyrone Thames (11254964), Alexander J. Bryer (8837516), Xin Qiao (1625608), Jaekyun Jeon (3699289), Ryan Weed (11254967), Kaylie Janicki (11254970), Bingwen Hu (1305561), Peter L. Gor’kov (1644127), Ivan Hung (1273608), Zhehong Gan (1635097), Juan R. Perilla (2638567), Bo Chen (32294)
سنة النشر: 2021
المجموعة: Smithsonian Institution: Digital Repository
مصطلحات موضوعية: Biophysics, Biochemistry, Medicine, Cell Biology, Infectious Diseases, Computational Biology, Biological Sciences not elsewhere classified, Chemical Sciences not elsewhere classified, Physical Sciences not elsewhere classified, C-terminal domain, cryoelectron tomography restraints, control assembly curvature, 12 pentamers, Molecular Switch, capsid proteins, residue, interdomain linker, Retroviral Capsid Assembly, Rous sarcoma virus, maturation step, polymorphic capsids, RSV CA, hexameric lattice, capsid assembly, conformation, CA T, 1 capsid, dynamics simulations, N-terminal domain, NMR
الوصف: During the maturation step, the retroviral capsid proteins (CAs) assemble into polymorphic capsids. Their acute curvature is largely determined by 12 pentamers inserted into the hexameric lattice. However, how the CA switches its conformation to control assembly curvature remains unclear. We report the high-resolution structural model of the Rous sarcoma virus (RSV) CA T = 1 capsid, established by molecular dynamics simulations combining solid-state NMR and prior cryoelectron tomography restraints. Comparing this with our previous model of the RSV CA tubular assembly, we identify the key residues for dictating the incorporation of acute curvatures. These residues undergo large torsion angle changes, resulting in a 34° rotation of the C-terminal domain relative to its N-terminal domain around the flexible interdomain linker, without substantial changes of either the conformation of individual domains or the assembly contact interfaces. This knowledge provides new insights to help decipher the mechanism of the retroviral capsid assembly.
نوع الوثيقة: dataset
اللغة: unknown
Relation: https://figshare.com/articles/media/Curvature_of_the_Retroviral_Capsid_Assembly_Is_Modulated_by_a_Molecular_Switch/15142148
DOI: 10.1021/acs.jpclett.1c01769.s003
الاتاحة: https://doi.org/10.1021/acs.jpclett.1c01769.s003
Rights: CC BY-NC 4.0
رقم الانضمام: edsbas.188370E
قاعدة البيانات: BASE
الوصف
DOI:10.1021/acs.jpclett.1c01769.s003