3GZF

Structure of the C-terminal domain of nsp4 from Feline Coronavirus

Summary for 3GZF

• Entry DOI: 10.2210/pdb3gzf/pdb
• Descriptor: Replicase polyprotein 1ab, SULFATE ION (3 entities in total)
• Functional Keywords: coronavirus, fcov, nsp4, viral protein
• Biological source: Feline coronavirus
• 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): Q98VG9
• Total number of polymer chains: 5
• Total formula weight: 53982.46

Authors

Manolaridis, I.,Wojdyla, J.A.,Panjikar, S.,Snijder, E.J.,Gorbalenya, A.E.,Coutard, B.,Tucker, P.A. (deposition date: 2009-04-07, release date: 2009-08-18, Last modification date: 2024-03-20)

Primary citation

Manolaridis, I.,Wojdyla, J.A.,Panjikar, S.,Snijder, E.J.,Gorbalenya, A.E.,Berglind, H.,Nordlund, P.,Coutard, B.,Tucker, P.A.
Structure of the C-terminal domain of nsp4 from feline coronavirus
Acta Crystallogr.,Sect.D, 65:839-846, 2009

PubMed Abstract: Coronaviruses are a family of positive-stranded RNA viruses that includes important pathogens of humans and other animals. The large coronavirus genome (26-31 kb) encodes 15-16 nonstructural proteins (nsps) that are derived from two replicase polyproteins by autoproteolytic processing. The nsps assemble into the viral replication-transcription complex and nsp3, nsp4 and nsp6 are believed to anchor this enzyme complex to modified intracellular membranes. The largest part of the coronavirus nsp4 subunit is hydrophobic and is predicted to be embedded in the membranes. In this report, a conserved C-terminal domain ( approximately 100 amino-acid residues) has been delineated that is predicted to face the cytoplasm and has been isolated as a soluble domain using library-based construct screening. A prototypical crystal structure at 2.8 A resolution was obtained using nsp4 from feline coronavirus. Unmodified and SeMet-substituted proteins were crystallized under similar conditions, resulting in tetragonal crystals that belonged to space group P4(3). The phase problem was initially solved by single isomorphous replacement with anomalous scattering (SIRAS), followed by molecular replacement using a SIRAS-derived composite model. The structure consists of a single domain with a predominantly alpha-helical content displaying a unique fold that could be engaged in protein-protein interactions.

PubMed: 19622868
DOI: 10.1107/S0907444909018253

Experimental method

X-RAY DIFFRACTION (2.756 Å)