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1QOL

STRUCTURE OF THE FMDV LEADER PROTEASE

Summary for 1QOL
Entry DOI10.2210/pdb1qol/pdb
Related1QMY 1QQP
DescriptorPROTEASE (NONSTRUCTURAL PROTEIN P20A), 1,2-ETHANEDIOL, CHLORIDE ION (3 entities in total)
Functional Keywordshydrolase, sulfhydryl proteinase, picornaviral proteinase
Biological sourceFOOT-AND-MOUTH DISEASE VIRUS
Total number of polymer chains8
Total formula weight158526.33
Authors
Guarne, A.,Tormo, J.,Kirchweger, R.,Pfistermueller, D.,Skern, T.,Fita, I. (deposition date: 1999-11-13, release date: 2000-11-10, Last modification date: 2024-10-16)
Primary citationGuarne, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

238268

数据于2025-07-02公开中

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