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[[Image:1vzv.gif|left|200px]]<br /><applet load="1vzv" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1vzv, resolution 3.0&Aring;" />
'''STRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASE'''<br />


==Overview==
==STRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASE==
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.
<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 [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_3 Human alphaherpesvirus 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 [https://proteopedia.org/fgij/fg.htm?mol=1VZV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzv OCA], [https://pdbe.org/1vzv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vzv RCSB], [https://www.ebi.ac.uk/pdbsum/1vzv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vzv ProSAT]</span></td></tr>
</table>
== Function ==
[https://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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vz/1vzv_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/main_output.php?pdb_ID=1vzv ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1VZV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Varicella-zoster_virus_(isolate_40a2) Varicella-zoster virus (isolate 40a2)]. Known structural/functional Site: <scene name='pdbsite=CAT:Catalytic Triad'>CAT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VZV OCA].
*[[Virus protease 3D structures|Virus protease 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9096314 9096314]
[[Category: Human alphaherpesvirus 3]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Varicella-zoster virus (isolate 40a2)]]
[[Category: Abdel-Meguid SS]]
[[Category: Abdel-Meguid, S.S.]]
[[Category: Culp JS]]
[[Category: Culp, J.S.]]
[[Category: Debouck C]]
[[Category: Debouck, C.]]
[[Category: Jason CA]]
[[Category: Jason, C.A.]]
[[Category: Qiu X]]
[[Category: Qiu, X.]]
[[Category: Richardson SB]]
[[Category: Richardson, S.B.]]
[[Category: Smith WW]]
[[Category: Smith, W.W.]]
[[Category: coat protein]]
[[Category: hydrolase]]
[[Category: serine protease]]
[[Category: varicella-zoster virus]]
[[Category: viral protease]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:24:47 2007''

Latest revision as of 11:47, 14 February 2024

STRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASESTRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASE

Structural highlights

1vzv is a 1 chain structure with sequence from Human alphaherpesvirus 3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

1vzv, resolution 3.00Å

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