4ASH

Crystal structure of the NS6 protease from murine norovirus 1

4ASH の概要

• エントリーDOI: 10.2210/pdb4ash/pdb
• 分子名称: NS6 PROTEASE (2 entities in total)
• 機能のキーワード: hydrolase, trypsin-like, calicivirus
• 由来する生物種: MURINE NOROVIRUS 1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38736.26

構造登録者

Leen, E.N.,Baeza, G.,Curry, S. (登録日: 2012-05-01, 公開日: 2012-05-16, 最終更新日: 2023-12-20)

主引用文献

Leen, E.N.,Baeza, G.,Curry, S.
Structure of a Murine Norovirus Ns6 Protease-Product Complex Revealed by Adventitious Crystallisation.
Plos One, 7:38723-, 2012

PubMed Abstract: Murine noroviruses have emerged as a valuable tool for investigating the molecular basis of infection and pathogenesis of the closely related human noroviruses, which are the major cause of non-bacterial gastroenteritis. The replication of noroviruses relies on the proteolytic processing of a large polyprotein precursor into six non-structural proteins (NS1-2, NS3, NS4, NS5, NS6(pro), NS7(pol)) by the virally-encoded NS6 protease. We report here the crystal structure of MNV NS6(pro), which has been determined to a resolution of 1.6 Å. Adventitiously, the crystal contacts are mediated in part by the binding of the C-terminus of NS6(pro) within the peptide-binding cleft of a neighbouring molecule. This insertion occurs for both molecules in the asymmetric unit of the crystal in a manner that is consistent with physiologically-relevant binding, thereby providing two independent views of a protease-peptide complex. Since the NS6(pro) C-terminus is formed in vivo by NS6(pro) processing, these crystal contacts replicate the protease-product complex that is formed immediately following cleavage of the peptide bond at the NS6-NS7 junction. The observed mode of binding of the C-terminal product peptide yields new insights into the structural basis of NS6(pro) specificity.

PubMed: 22685603
DOI: 10.1371/JOURNAL.PONE.0038723

実験手法

X-RAY DIFFRACTION (1.578 Å)