5DUS

Crystal structure of MERS-CoV macro domain in complex with ADP-ribose

5DUS の概要

• エントリーDOI: 10.2210/pdb5dus/pdb
• 分子名称: ORF1a, ADENOSINE-5-DIPHOSPHORIBOSE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: ligand, complex, macro domain, adp-ribose, viral protein
• 由来する生物種: Middle East respiratory syndrome coronavirus
• 細胞内の位置: Host membrane ; Multi-pass membrane protein : T2B9G2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18805.28

構造登録者

Cho, C.-C.,Lin, M.-H.,Chuang, C.-Y.,Hsu, C.-H. (登録日: 2015-09-20, 公開日: 2016-01-13, 最終更新日: 2024-03-20)

主引用文献

Cho, C.-C.,Lin, M.-H.,Chuang, C.-Y.,Hsu, C.-H.
Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module: CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES
J.Biol.Chem., 291:4894-4902, 2016

PubMed Abstract: The newly emerging Middle East respiratory syndrome coronavirus (MERS-CoV) encodes the conserved macro domain within non-structural protein 3. However, the precise biochemical function and structure of the macro domain is unclear. Using differential scanning fluorimetry and isothermal titration calorimetry, we characterized the MERS-CoV macro domain as a more efficient adenosine diphosphate (ADP)-ribose binding module than macro domains from other CoVs. Furthermore, the crystal structure of the MERS-CoV macro domain was determined at 1.43-Å resolution in complex with ADP-ribose. Comparison of macro domains from MERS-CoV and other human CoVs revealed structural differences in the α1 helix alters how the conserved Asp-20 interacts with ADP-ribose and may explain the efficient binding of the MERS-CoV macro domain to ADP-ribose. This study provides structural and biophysical bases to further evaluate the role of the MERS-CoV macro domain in the host response via ADP-ribose binding but also as a potential target for drug design.

PubMed: 26740631
DOI: 10.1074/jbc.M115.700542

実験手法

X-RAY DIFFRACTION (1.432 Å)