2bhg
From Proteopedia
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| - | [[Image:2bhg.gif|left|200px]] | + | [[Image:2bhg.gif|left|200px]] |
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| - | '''3C PROTEASE FROM TYPE A10(61) FOOT-AND-MOUTH DISEASE VIRUS''' | + | {{Structure |
| + | |PDB= 2bhg |SIZE=350|CAPTION= <scene name='initialview01'>2bhg</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Picornain_3C Picornain 3C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.28 3.4.22.28] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''3C PROTEASE FROM TYPE A10(61) FOOT-AND-MOUTH DISEASE VIRUS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BHG is a [ | + | 2BHG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BHG OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity., Birtley JR, Knox SR, Jaulent AM, Brick P, Leatherbarrow RJ, Curry S, J Biol Chem. 2005 Mar 25;280(12):11520-7. Epub 2005 Jan 14. PMID:[http:// | + | Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity., Birtley JR, Knox SR, Jaulent AM, Brick P, Leatherbarrow RJ, Curry S, J Biol Chem. 2005 Mar 25;280(12):11520-7. Epub 2005 Jan 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15654079 15654079] |
[[Category: Foot-and-mouth disease virus]] | [[Category: Foot-and-mouth disease virus]] | ||
[[Category: Picornain 3C]] | [[Category: Picornain 3C]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 16:01:59 2008'' |
Revision as of 14:02, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Activity: | Picornain 3C, with EC number 3.4.22.28 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
3C PROTEASE FROM TYPE A10(61) FOOT-AND-MOUTH DISEASE VIRUS
Overview
Foot-and-mouth disease virus (FMDV) causes a widespread and economically devastating disease of domestic livestock. Although FMDV vaccines are available, political and technical problems associated with their use are driving a renewed search for alternative methods of disease control. The viral RNA genome is translated as a single polypeptide precursor that must be cleaved into functional proteins by virally encoded proteases. 10 of the 13 cleavages are performed by the highly conserved 3C protease (3C(pro)), making the enzyme an attractive target for antiviral drugs. We have developed a soluble, recombinant form of FMDV 3C(pro), determined the crystal structure to 1.9-angstroms resolution, and analyzed the cleavage specificity of the enzyme. The structure indicates that FMDV 3C(pro) adopts a chymotrypsin-like fold and possesses a Cys-His-Asp catalytic triad in a similar conformation to the Ser-His-Asp triad conserved in almost all serine proteases. This observation suggests that the dyad-based mechanisms proposed for this class of cysteine proteases need to be reassessed. Peptide cleavage assays revealed that the recognition sequence spans at least four residues either side of the scissile bond (P4-P4') and that FMDV 3C(pro) discriminates only weakly in favor of P1-Gln over P1-Glu, in contrast to other 3C(pro) enzymes that strongly favor P1-Gln. The relaxed specificity may be due to the unexpected absence in FMDV 3C(pro) of an extended beta-ribbon that folds over the substrate binding cleft in other picornavirus 3C(pro) structures. Collectively, these results establish a valuable framework for the development of FMDV 3C(pro) inhibitors.
About this Structure
2BHG is a Single protein structure of sequence from Foot-and-mouth disease virus. Full crystallographic information is available from OCA.
Reference
Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity., Birtley JR, Knox SR, Jaulent AM, Brick P, Leatherbarrow RJ, Curry S, J Biol Chem. 2005 Mar 25;280(12):11520-7. Epub 2005 Jan 14. PMID:15654079
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Categories: Foot-and-mouth disease virus | Picornain 3C | Single protein | Birtley, J R. | Brick, P. | Curry, S. | Capsid protein | Chymotrypsin-like cysteine protease | Core protein | Covalent protein-rna linkage | Hydrolase | Lipoprotein | Myristate | Polyprotein | Protease | Rna-directed rna polymerase | Thiol protease | Transferase
