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1q31

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Revision as of 08:18, 24 February 2018

Crystal Structure of the Tobacco Etch Virus Protease C151A mutant

Structural highlights

1q31 is a 2 chain structure with sequence from Tev. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1lvb, 1lvm
Activity:	Nuclear-inclusion-a endopeptidase, with EC number 3.4.22.44
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[POLG_TEV] Capsid protein: involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.^[1] ^[2] Nuclear inclusion protein B: an RNA-dependent RNA polymerase that plays an essential role in the virus replication.^[3] ^[4] Helper component proteinase: required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.^[5] ^[6] Cytoplasmic inclusion protein: has helicase activity. It may be involved in replication.^[7] ^[8] Both 6K peptides are indispensable for virus replication (By similarity).^[9] ^[10] Nuclear inclusion protein A: has RNA-binding and proteolytic activities.^[11] ^[12]

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

Tobacco etch virus (TEV) protease is a cysteine protease exhibiting stringent sequence specificity. The enzyme is widely used in biotechnology for the removal of the affinity tags from recombinant fusion proteins. Crystal structures of two TEV protease mutants as complexes with a substrate and a product peptide provided the first insight into the mechanism of substrate specificity of this enzyme. We now report a 2.7A crystal structure of a full-length inactive C151A mutant protein crystallised in the absence of peptide. The structure reveals the C terminus of the protease bound to the active site. In addition, we determined dissociation constants of TEV protease substrate and product peptides using isothermal titration calorimetry for various forms of this enzyme. Data suggest that TEV protease could be inhibited by the peptide product of autolysis. Separate modes of recognition for native substrates and the site of TEV protease self-cleavage are proposed.

Crystal structure of tobacco etch virus protease shows the protein C terminus bound within the active site.,Nunn CM, Jeeves M, Cliff MJ, Urquhart GT, George RR, Chao LH, Tscuchia Y, Djordjevic S J Mol Biol. 2005 Jul 1;350(1):145-55. PMID:15919091^[13]

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

References

↑ Blanc S, Ammar ED, Garcia-Lampasona S, Dolja VV, Llave C, Baker J, Pirone TP. Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets. J Gen Virol. 1998 Dec;79 ( Pt 12):3119-22. PMID:9880030
↑ Kasschau KD, Carrington JC. Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro. Virology. 2001 Jun 20;285(1):71-81. PMID:11414807 doi:http://dx.doi.org/10.1006/viro.2001.0901
↑ Blanc S, Ammar ED, Garcia-Lampasona S, Dolja VV, Llave C, Baker J, Pirone TP. Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets. J Gen Virol. 1998 Dec;79 ( Pt 12):3119-22. PMID:9880030
↑ Kasschau KD, Carrington JC. Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro. Virology. 2001 Jun 20;285(1):71-81. PMID:11414807 doi:http://dx.doi.org/10.1006/viro.2001.0901
↑ Blanc S, Ammar ED, Garcia-Lampasona S, Dolja VV, Llave C, Baker J, Pirone TP. Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets. J Gen Virol. 1998 Dec;79 ( Pt 12):3119-22. PMID:9880030
↑ Kasschau KD, Carrington JC. Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro. Virology. 2001 Jun 20;285(1):71-81. PMID:11414807 doi:http://dx.doi.org/10.1006/viro.2001.0901
↑ Blanc S, Ammar ED, Garcia-Lampasona S, Dolja VV, Llave C, Baker J, Pirone TP. Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets. J Gen Virol. 1998 Dec;79 ( Pt 12):3119-22. PMID:9880030
↑ Kasschau KD, Carrington JC. Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro. Virology. 2001 Jun 20;285(1):71-81. PMID:11414807 doi:http://dx.doi.org/10.1006/viro.2001.0901
↑ Blanc S, Ammar ED, Garcia-Lampasona S, Dolja VV, Llave C, Baker J, Pirone TP. Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets. J Gen Virol. 1998 Dec;79 ( Pt 12):3119-22. PMID:9880030
↑ Kasschau KD, Carrington JC. Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro. Virology. 2001 Jun 20;285(1):71-81. PMID:11414807 doi:http://dx.doi.org/10.1006/viro.2001.0901
↑ Blanc S, Ammar ED, Garcia-Lampasona S, Dolja VV, Llave C, Baker J, Pirone TP. Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets. J Gen Virol. 1998 Dec;79 ( Pt 12):3119-22. PMID:9880030
↑ Kasschau KD, Carrington JC. Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro. Virology. 2001 Jun 20;285(1):71-81. PMID:11414807 doi:http://dx.doi.org/10.1006/viro.2001.0901
↑ Nunn CM, Jeeves M, Cliff MJ, Urquhart GT, George RR, Chao LH, Tscuchia Y, Djordjevic S. Crystal structure of tobacco etch virus protease shows the protein C terminus bound within the active site. J Mol Biol. 2005 Jul 1;350(1):145-55. PMID:15919091 doi:10.1016/j.jmb.2005.04.013

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q31"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the Tobacco Etch Virus Protease C151A mutant==
 <StructureSection load='1q31' size='340' side='right' caption='[[1q31]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lvb|1lvb]], [[1lvm|1lvm]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nuclear-inclusion-a_endopeptidase Nuclear-inclusion-a endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.44 3.4.22.44] </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=1q31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q31 OCA], [http://pdbe.org/1q31 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q31 RCSB], [http://www.ebi.ac.uk/pdbsum/1q31 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=1q31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q31 OCA], [http://pdbe.org/1q31 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q31 RCSB], [http://www.ebi.ac.uk/pdbsum/1q31 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q31 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q3/1q31_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q3/1q31_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1q31 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 32: / Line 33: @@
 ==See Also==
 *[[Ashley Steere/Tobacco Etch Virus (TEV) Protease|Ashley Steere/Tobacco Etch Virus (TEV) Protease]]
-*[[Tobacco Etch Virus (TEV) Protease|Tobacco Etch Virus (TEV) Protease]]
 == References ==
 <references/>

1q31

From Proteopedia

Revision as of 08:18, 24 February 2018

Crystal Structure of the Tobacco Etch Virus Protease C151A mutant

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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