2AHM

Crystal structure of SARS-CoV super complex of non-structural proteins: the hexadecamer

Summary for 2AHM

• Entry DOI: 10.2210/pdb2ahm/pdb
• Descriptor: Replicase polyprotein 1ab, light chain, Replicase polyprotein 1ab, heavy chain, GLYCEROL, ... (5 entities in total)
• Functional Keywords: sars-cov, coronavirus, non-structural protein, nsp7, nsp8, super-complex, hexadecamer, viral protein, replication
• Biological source: SARS coronavirus; More
• Cellular location: Non-structural protein 3: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 4: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 6: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 7: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 8: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 9: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 10: Host cytoplasm, host perinuclear region (By similarity). Helicase: Host endoplasmic reticulum-Golgi intermediate compartment (Potential). Uridylate-specific endoribonuclease: Host cytoplasm, host perinuclear region (By similarity): P59641 P59641
• Total number of polymer chains: 8
• Total formula weight: 128507.40

Authors

Zhai, Y.J.,Sun, F.,Bartlam, M.,Rao, Z. (deposition date: 2005-07-28, release date: 2005-11-15, Last modification date: 2024-03-13)

Primary citation

Zhai, Y.J.,Sun, F.,Li, X.,Pang, H.,Xu, X.,Bartlam, M.,Rao, Z.
Insights into SARS-CoV transcription and replication from the structure of the nsp7-nsp8 hexadecamer
NAT.STRUCT.MOL.BIOL., 12:980-986, 2005

PubMed 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.

PubMed: 16228002
DOI: 10.1038/nsmb999

Experimental method

X-RAY DIFFRACTION (2.4 Å)