2XYR

Crystal structure of the nsp16 nsp10 SARS coronavirus complex

Summary for 2XYR

• Entry DOI: 10.2210/pdb2xyr/pdb
• Descriptor: PUTATIVE 2'-O-METHYL TRANSFERASE, NON-STRUCTURAL PROTEIN 10, SODIUM ION, ... (8 entities in total)
• Functional Keywords: transferase-viral protein complex, rossmann fold, transferase/viral protein
• Biological source: SARS CORONAVIRUS; More
• Cellular location: Papain-like proteinase: Host membrane; Multi-pass membrane protein. Non-structural protein 4: Host membrane; Multi-pass membrane protein. Non-structural protein 6: Host membrane ; Multi-pass membrane protein . Non-structural protein 7: Host cytoplasm, host perinuclear region . Non-structural protein 8: Host cytoplasm, host perinuclear region . Non-structural protein 9: Host cytoplasm, host perinuclear region . Non-structural protein 10: Host cytoplasm, host perinuclear region . Helicase: Host endoplasmic reticulum-Golgi intermediate compartment . Uridylate-specific endoribonuclease: Host cytoplasm, host perinuclear region : P0C6X7 P0C6X7
• Total number of polymer chains: 2
• Total formula weight: 46655.40

Authors

Decroly, E.,Debarnot, C.,Ferron, F.,Bouvet, M.,Coutard, B.,Imbert, I.,Gluais, L.,Papageorgiou, N.,Ortiz-Lombardia, M.,Lescar, J.,Canard, B. (deposition date: 2010-11-18, release date: 2011-10-26, Last modification date: 2023-12-20)

Primary citation

Decroly, E.,Debarnot, C.,Ferron, F.,Bouvet, M.,Coutard, B.,Imbert, I.,Gluais, L.,Papageorgiou, N.,Sharff, A.,Bricogne, G.,Ortiz-Lombardia, M.,Lescar, J.,Canard, B.
Crystal Structure and Functional Analysis of the Sars-Coronavirus RNA CAP 2'-O-Methyltransferase Nsp10/Nsp16 Complex.
Plos Pathog., 7:2059-, 2011

PubMed Abstract: Cellular and viral S-adenosylmethionine-dependent methyltransferases are involved in many regulated processes such as metabolism, detoxification, signal transduction, chromatin remodeling, nucleic acid processing, and mRNA capping. The Severe Acute Respiratory Syndrome coronavirus nsp16 protein is a S-adenosylmethionine-dependent (nucleoside-2'-O)-methyltransferase only active in the presence of its activating partner nsp10. We report the nsp10/nsp16 complex structure at 2.0 Å resolution, which shows nsp10 bound to nsp16 through a ∼930 Ų surface area in nsp10. Functional assays identify key residues involved in nsp10/nsp16 association, and in RNA binding or catalysis, the latter likely through a SN2-like mechanism. We present two other crystal structures, the inhibitor Sinefungin bound in the S-adenosylmethionine binding pocket and the tighter complex nsp10(Y96F)/nsp16, providing the first structural insight into the regulation of RNA capping enzymes in +RNA viruses.

PubMed: 21637813
DOI: 10.1371/JOURNAL.PPAT.1002059

Experimental method

X-RAY DIFFRACTION (2.5 Å)