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2bhg

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Revision as of 11:14, 11 September 2015

3C PROTEASE FROM TYPE A10(61) FOOT-AND-MOUTH DISEASE VIRUS

Structural highlights

2bhg is a 2 chain structure with sequence from Fmdv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Activity:	Picornain 3C, with EC number 3.4.22.28
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Birtley JR, Knox SR, Jaulent AM, Brick P, Leatherbarrow RJ, Curry S. Crystal structure of foot-and-mouth disease virus 3C protease. New insights into catalytic mechanism and cleavage specificity. J Biol Chem. 2005 Mar 25;280(12):11520-7. Epub 2005 Jan 14. PMID:15654079 doi:10.1074/jbc.M413254200

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bhg"

@@ Line 2: / Line 2: @@
 <StructureSection load='2bhg' size='340' side='right' caption='[[2bhg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bhg]] is a 2 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BHG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bhg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Fmdv Fmdv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BHG FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bhg RCSB], [http://www.ebi.ac.uk/pdbsum/2bhg PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhg OCA], [http://pdbe.org/2bhg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bhg RCSB], [http://www.ebi.ac.uk/pdbsum/2bhg PDBsum]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 25: / Line 25: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2bhg" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 33: / Line 34: @@
 __TOC__
 </StructureSection>
-[[Category: Foot-and-mouth disease virus]]
+[[Category: Fmdv]]
 [[Category: Picornain 3C]]
 [[Category: Birtley, J R]]
@@ Line 42: / Line 43: @@
 [[Category: Core protein]]
 [[Category: Covalent protein-rna linkage]]
+[[Category: Foot-and-mouth disease virus]]
 [[Category: Hydrolase]]
 [[Category: Lipoprotein]]

2bhg

From Proteopedia

Revision as of 11:14, 11 September 2015

3C PROTEASE FROM TYPE A10(61) FOOT-AND-MOUTH DISEASE VIRUS

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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