1vzv

From Proteopedia

(Difference between revisions)

Revision as of 10:39, 10 September 2015

STRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASE

Structural highlights

1vzv is a 1 chain structure with sequence from Hhv-3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[SCAF_VZVD] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein 40 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein 40 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein 40. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein 40. Multimerizes in the nucleus such as protein 40 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).

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

Varicella-zoster virus (VZV), an alpha-herpes virus, is the causative agent of chickenpox, shingles, and postherpetic neuralgia. The three-dimensional crystal structure of the serine protease from VZV has been determined at 3.0-A resolution. The VZV protease is essential for the life cycle of the virus and is a potential target for therapeutic intervention. The structure reveals an overall fold that is similar to that recently reported for the serine protease from cytomegalovirus (CMV), a herpes virus of the beta subfamily. The VZV protease structure provides further evidence to support the finding that herpes virus proteases have a fold and active site distinct from other serine proteases. The VZV protease catalytic triad consists of a serine and two histidines. The distal histidine is proposed to properly orient the proximal histidine. The identification of an alpha-helical segment in the VZV protease that was mostly disordered in the CMV protease provides a better definition of the postulated active site cavity and reveals an elastase-like S' region. Structural differences between the VZV and CMV proteases also suggest potential differences in their oligomerization states.

Crystal structure of varicella-zoster virus protease.,Qiu X, Janson CA, Culp JS, Richardson SB, Debouck C, Smith WW, Abdel-Meguid SS Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):2874-9. PMID:9096314^[1]

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

References

↑ Qiu X, Janson CA, Culp JS, Richardson SB, Debouck C, Smith WW, Abdel-Meguid SS. Crystal structure of varicella-zoster virus protease. Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):2874-9. PMID:9096314

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/1vzv"

@@ Line 2: / Line 2: @@
 <StructureSection load='1vzv' size='340' side='right' caption='[[1vzv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1vzv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_3 Human herpesvirus 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VZV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1vzv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hhv-3 Hhv-3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VZV FirstGlance]. <br>
-</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=1vzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vzv RCSB], [http://www.ebi.ac.uk/pdbsum/1vzv PDBsum]</span></td></tr>
+</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=1vzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzv OCA], [http://pdbe.org/1vzv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vzv RCSB], [http://www.ebi.ac.uk/pdbsum/1vzv PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/VP40_VZVD VP40_VZVD]] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein 40 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein 40 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein 40. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity).  Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity).  Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein 40. Multimerizes in the nucleus such as protein 40 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).
+[[http://www.uniprot.org/uniprot/SCAF_VZVD SCAF_VZVD]] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein 40 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein 40 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein 40. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity).  Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity).  Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein 40. Multimerizes in the nucleus such as protein 40 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ 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 1vzv" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Human herpesvirus 3]]
+[[Category: Hhv-3]]
 [[Category: Abdel-Meguid, S S]]
 [[Category: Culp, J S]]

1vzv

From Proteopedia

Revision as of 10:39, 10 September 2015

STRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASE

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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