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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1lay]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cytomegalovirus Cytomegalovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LAY FirstGlance]. <br>
<table><tr><td colspan='2'>[[1lay]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cytomegalovirus Cytomegalovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LAY FirstGlance]. <br>
</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=1lay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lay OCA], [https://pdbe.org/1lay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lay RCSB], [https://www.ebi.ac.uk/pdbsum/1lay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lay ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#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=1lay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lay OCA], [https://pdbe.org/1lay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lay RCSB], [https://www.ebi.ac.uk/pdbsum/1lay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lay ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SCAF_HCMVA SCAF_HCMVA]] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein UL86 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein UL86. 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 UL86. Multimerizes in the nucleus such as protein UL86 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).  
[https://www.uniprot.org/uniprot/SCAF_HCMVA SCAF_HCMVA] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein UL86 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein UL86. 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 UL86. Multimerizes in the nucleus such as protein UL86 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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1lay 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=1lay ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human herpesviruses are responsible for a variety of diseases. They are divided into three subfamilies: alpha includes herpes simplex viruses (HSV-1 and HSV-2) and varicella-zoster virus (VZV); beta includes cytomegalovirus (CMV) and human herpesvirus-6 (HHV-6); and gamma includes Epstein-Barr virus (EBV). Each virus encodes a serine protease that is essential for its replication and is a potential target for therapeutic intervention. Human CMV is a ubiquitous opportunistic pathogen that can result in life-threatening infections in congenitally infected infants, immunocompromised individuals and immunosuppressed cancer or transplant patients. Here we report the crystal structure of human CMV protease at 2.5 angstroms resolution. The structure reveals a fold that has not been reported for any other serine protease, and an active site consisting of a novel catalytic triad in which the third member is a histidine instead of an aspartic acid, or possibly a catalytic tetrad consisting of a serine, two histidines and an aspartic acid. An unusual dimer interface that is important to the protease activity has also been identified.
Unique fold and active site in cytomegalovirus protease.,Qiu X, Culp JS, DiLella AG, Hellmig B, Hoog SS, Janson CA, Smith WW, Abdel-Meguid SS Nature. 1996 Sep 19;383(6597):275-9. PMID:8805707<ref>PMID:8805707</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1lay" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Virus protease 3D structures|Virus protease 3D structures]]
*[[Virus protease 3D structures|Virus protease 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cytomegalovirus]]
[[Category: Cytomegalovirus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Abdel-Meguid, S S]]
[[Category: Abdel-Meguid SS]]
[[Category: Culp, J S]]
[[Category: Culp JS]]
[[Category: Dilella, A G]]
[[Category: Dilella AG]]
[[Category: Hellmig, B]]
[[Category: Hellmig B]]
[[Category: Hoog, S S]]
[[Category: Hoog SS]]
[[Category: Jason, C A]]
[[Category: Jason CA]]
[[Category: Qiu, X]]
[[Category: Qiu X]]
[[Category: Smith, W W]]
[[Category: Smith WW]]
[[Category: Serine protease]]
[[Category: Viral protease]]
Retrieved from "https://proteopedia.org/1lay"