2XYV

Crystal structure of the nsp16 nsp10 SARS coronavirus complex

2XYV の概要

• エントリーDOI: 10.2210/pdb2xyv/pdb
• 関連するPDBエントリー: 1O5S 1P76 1P9T 1PA5 1PUK 1Q1X 1SXF 1UJ1 1UK2 1UK3 1UK4 1UW7 1WOF 1YSY 1Z1I 1Z1J 2A5A 2A5I 2A5K 2ACF 2AHM 2AMD 2AMQ 2BX3 2BX4 2C3S 2D2D 2V6N 2XYQ 2XYR
• 分子名称: PUTATIVE 2'-O-METHYL TRANSFERASE, NON-STRUCTURAL PROTEIN 10, SODIUM ION, ... (8 entities in total)
• 機能のキーワード: transferase-viral protein complex, rossmann fold, transferase/viral protein
• 由来する生物種: SARS CORONAVIRUS; 詳細
• 細胞内の位置: 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
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46688.40

構造登録者

Decroly, E.,Debarnot, C.,Ferron, F.,Bouvet, M.,Coutard, B.,Imbert, I.,Gluais, L.,Papageorgiou, N.,Ortiz-Lombardia, M.,Lescar, J.,Canard, B. (登録日: 2010-11-19, 公開日: 2011-10-26, 最終更新日: 2023-12-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.06 Å)