1qol
From Proteopedia
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| - | [[Image:1qol.gif|left|200px]] | + | [[Image:1qol.gif|left|200px]] |
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| - | '''STRUCTURE OF THE FMDV LEADER PROTEASE''' | + | {{Structure |
| + | |PDB= 1qol |SIZE=350|CAPTION= <scene name='initialview01'>1qol</scene>, resolution 3.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF THE FMDV LEADER PROTEASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QOL is a [ | + | 1QOL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Polg_fmdvo Polg_fmdvo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOL OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for self-processing and eIF4G recognition., Guarne A, Tormo J, Kirchweger R, Pfistermueller D, Fita I, Skern T, EMBO J. 1998 Dec 15;17(24):7469-79. PMID:[http:// | + | Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for self-processing and eIF4G recognition., Guarne A, Tormo J, Kirchweger R, Pfistermueller D, Fita I, Skern T, EMBO J. 1998 Dec 15;17(24):7469-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9857201 9857201] |
[[Category: Polg_fmdvo]] | [[Category: Polg_fmdvo]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sulfhydryl proteinase]] | [[Category: sulfhydryl proteinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:40:30 2008'' |
Revision as of 11:40, 20 March 2008
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| , resolution 3.00Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE FMDV LEADER PROTEASE
Overview
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.
About this Structure
1QOL is a Single protein structure of sequence from Polg_fmdvo. Full crystallographic information is available from OCA.
Reference
Structure of the foot-and-mouth disease virus leader protease: a papain-like fold adapted for self-processing and eIF4G recognition., Guarne A, Tormo J, Kirchweger R, Pfistermueller D, Fita I, Skern T, EMBO J. 1998 Dec 15;17(24):7469-79. PMID:9857201
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