1QOL

STRUCTURE OF THE FMDV LEADER PROTEASE

1QOL の概要

• エントリーDOI: 10.2210/pdb1qol/pdb
• 関連するPDBエントリー: 1QMY 1QQP
• 分子名称: PROTEASE (NONSTRUCTURAL PROTEIN P20A), 1,2-ETHANEDIOL, CHLORIDE ION (3 entities in total)
• 機能のキーワード: hydrolase, sulfhydryl proteinase, picornaviral proteinase
• 由来する生物種: FOOT-AND-MOUTH DISEASE VIRUS
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 158526.33

構造登録者

Guarne, A.,Tormo, J.,Kirchweger, R.,Pfistermueller, D.,Skern, T.,Fita, I. (登録日: 1999-11-13, 公開日: 2000-11-10, 最終更新日: 2024-10-16)

主引用文献

Guarne, A.,Tormo, J.,Kirchweger, R.,Pfistermueller, D.,Fita, I.,Skern, T.
Structure of the Foot-and-Mouth Disease Virus Leader Protease: A Papain-Like Fold Adapted for Self-Processing and Eif4G Recognition.
Embo J., 17:7469-, 1998

PubMed Abstract: The leader protease of foot-and-mouth disease virus, as well as cleaving itself from the nascent viral polyprotein, disables host cell protein synthesis by specific proteolysis of a cellular protein: the eukaryotic initiation factor 4G (eIF4G). The crystal structure of the leader protease presented here comprises a globular catalytic domain reminiscent of that of cysteine proteases of the papain superfamily, and a flexible C-terminal extension found intruding into the substrate-binding site of an adjacent molecule. Nevertheless, the relative disposition of this extension and the globular domain to each other supports intramolecular self-processing. The different sequences of the two substrates cleaved during viral replication, the viral polyprotein (at LysLeuLys/GlyAlaGly) and eIF4G (at AsnLeuGly/ArgThrThr), appear to be recognized by distinct features in a narrow, negatively charged groove traversing the active centre. The structure illustrates how the prototype papain fold has been adapted to the requirements of an RNA virus. Thus, the protein scaffold has been reduced to a minimum core domain, with the active site being modified to increase specificity. Furthermore, surface features have been developed which enable C-terminal self-processing from the viral polyprotein.

PubMed: 9857201
DOI: 10.1093/EMBOJ/17.24.7469

実験手法

X-RAY DIFFRACTION (3 Å)