2LNC

Solution NMR structure of Norwalk virus protease

2LNC の概要

• エントリーDOI: 10.2210/pdb2lnc/pdb
• NMR情報: BMRB: 17523
• 分子名称: 3C-like protease (1 entity in total)
• 機能のキーワード: viral protease, chymotrypsin-like protease, hydrolase, calicivirus
• 由来する生物種: Norovirus
• 細胞内の位置: Protein p48: Host membrane; Single-pass membrane protein (Potential). NTPase: Host membrane; Single-pass membrane protein (Potential). Protein p22: Host membrane; Single-pass membrane protein (Potential): Q83883
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20126.13

構造登録者

Takahashi, D.,Hiromasa, Y.,Kim, Y.,Anbanandam, A.,Chang, K.,Prakash, O. (登録日: 2011-12-22, 公開日: 2012-12-26, 最終更新日: 2024-05-01)

主引用文献

Takahashi, D.,Hiromasa, Y.,Kim, Y.,Anbanandam, A.,Yao, X.,Chang, K.O.,Prakash, O.
Structural and dynamics characterization of norovirus protease.
Protein Sci., 22:347-357, 2013

PubMed Abstract: Norovirus protease is an essential enzyme for proteolytic maturation of norovirus nonstructural proteins and has been implicated as a potential target for antiviral drug development. Although X-ray structural studies of the protease give us wealth of structural information including interactions of the protease with its substrate and dimeric overall structure, the role of protein dynamics in the substrate recognition and the biological relevance of the protease dimer remain unclear. Here we determined the solution NMR structure of the 3C-like protease from Norwalk virus (NV 3CLpro), a prototype strain of norovirus, and analyzed its backbone dynamics and hydrodynamic behavior in solution. ¹⁵N spin relaxation and analytical ultracentrifugation analyses demonstrate that NV 3CLpro is predominantly a monomer in solution. Solution structure of NV 3CLpro shows significant structural variation in C-terminal domain compared with crystal structures and among lower energy structure ensembles. Also, ¹⁵N spin relaxation and Carr-Purcell-Meiboom-Gill (CPMG)-based relaxation dispersion analyses reveal the dynamic properties of residues in the C-terminal domain over a wide range of timescales. In particular, the long loop spanning residues T123-G133 show fast motion (ps-ns), and the residues in the bII-cII region forming the large hydrophobic pocket (S2 site) undergo conformational exchanges on slower timescales (μs-ms), suggesting their important role in substrate recognition.

PubMed: 23319456
DOI: 10.1002/pro.2215

実験手法

SOLUTION NMR