Insights Into SARS-CoV Transcription and Replication From the Structure of the nsp7-nsp8 Hexadecamer

Nat Struct Mol Biol. 2005 Nov;12(11):980-6. doi: 10.1038/nsmb999.

Abstract

Coronavirus replication and transcription machinery involves multiple virus-encoded nonstructural proteins (nsp). We report the crystal structure of the hexadecameric nsp7-nsp8 supercomplex from the severe acute respiratory syndrome coronavirus at 2.4-angstroms resolution. nsp8 has a novel 'golf-club' fold with two conformations. The supercomplex is a unique hollow, cylinder-like structure assembled from eight copies of nsp8 and held tightly together by eight copies of nsp7. With an internal diameter of approximately 30 angstroms, the central channel has dimensions and positive electrostatic properties favorable for nucleic acid binding, implying that its role is to confer processivity on RNA-dependent RNA polymerase.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Crystallization
  • DNA Primers
  • Electrophoretic Mobility Shift Assay
  • Microscopy, Electron
  • Models, Molecular*
  • Molecular Sequence Data
  • Multiprotein Complexes / chemistry*
  • Multiprotein Complexes / metabolism
  • Multiprotein Complexes / ultrastructure
  • RNA Replicase / metabolism
  • SARS Virus / genetics*
  • SARS Virus / physiology
  • Sequence Analysis, DNA
  • Structure-Activity Relationship
  • Transcription, Genetic / genetics*
  • Viral Nonstructural Proteins / chemistry*
  • Viral Nonstructural Proteins / metabolism
  • Viral Nonstructural Proteins / ultrastructure
  • Virus Replication / genetics
  • Virus Replication / physiology*

Substances

  • DNA Primers
  • Multiprotein Complexes
  • Viral Nonstructural Proteins
  • RNA Replicase

Associated data

  • PDB/2AHM