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| | <StructureSection load='2wpo' size='340' side='right'caption='[[2wpo]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='2wpo' size='340' side='right'caption='[[2wpo]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wpo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hcmv Hcmv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WPO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WPO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wpo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_betaherpesvirus_5 Human betaherpesvirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WPO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=01E:(2S)-2-(3,3-DIMETHYLBUTANOYLAMINO)-N-[(2S)-1-[[(2S,3S)-3-HYDROXY-4-[(4-IODOPHENYL)METHYLAMINO]-4-OXO-BUTAN-2-YL]AMINO]-1,4-DIOXO-4-PYRROL-1-YL-BUTAN-2-YL]-3,3-DIMETHYL-BUTANAMIDE'>01E</scene></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]] 2.7Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2wpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wpo OCA], [http://pdbe.org/2wpo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wpo RCSB], [http://www.ebi.ac.uk/pdbsum/2wpo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wpo ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=01E:(2S)-2-(3,3-DIMETHYLBUTANOYLAMINO)-N-[(2S)-1-[[(2S,3S)-3-HYDROXY-4-[(4-IODOPHENYL)METHYLAMINO]-4-OXO-BUTAN-2-YL]AMINO]-1,4-DIOXO-4-PYRROL-1-YL-BUTAN-2-YL]-3,3-DIMETHYL-BUTANAMIDE'>01E</scene></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=2wpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wpo OCA], [https://pdbe.org/2wpo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wpo RCSB], [https://www.ebi.ac.uk/pdbsum/2wpo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wpo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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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| | ==See Also== | | ==See Also== |
| - | *[[Virus proteases 3D strutures|Virus proteases 3D strutures]] | + | *[[Virus protease 3D structures|Virus protease 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hcmv]] | + | [[Category: Human betaherpesvirus 5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Deziel, R]] | + | [[Category: Deziel R]] |
| - | [[Category: Lagace, L]] | + | [[Category: Lagace L]] |
| - | [[Category: Massariol, M J]] | + | [[Category: Massariol M-J]] |
| - | [[Category: Qian, C]] | + | [[Category: Qian C]] |
| - | [[Category: Tong, L]] | + | [[Category: Tong L]] |
| - | [[Category: Yoakim, C]] | + | [[Category: Yoakim C]] |
| - | [[Category: Coat protein]]
| + | |
| - | [[Category: Hydrolase-hydrolase inhibitor complex]]
| + | |
| - | [[Category: Serine protease]]
| + | |
| - | [[Category: Viral protease]]
| + | |
| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Human cytomegalovirus (HCMV) protease belongs to a new class of serine proteases, with a unique polypeptide backbone fold. The crystal structure of the protease in complex with a peptidomimetic inhibitor (based on the natural substrates and covering the P4 to P1' positions) has been determined at 2.7 A resolution. The inhibitor is bound in an extended conformation, forming an anti-parallel beta-sheet with the protease. The P3 and P1 side chains are less accessible to solvent, whereas the P4 and P2 side chains are more exposed. The inhibitor binding mode shows significant similarity to those observed for peptidomimetic inhibitors or substrates of other classes of serine proteases (chymotrypsin and subtilisin). HCMV protease therefore represents example of convergent evolution. In addition, large conformational differences relative to the structure of the free enzyme are observed, which may be important for inhibitor binding.
Conserved mode of peptidomimetic inhibition and substrate recognition of human cytomegalovirus protease.,Tong L, Qian C, Massariol MJ, Deziel R, Yoakim C, Lagace L Nat Struct Biol. 1998 Sep;5(9):819-26. PMID:9731777[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tong L, Qian C, Massariol MJ, Deziel R, Yoakim C, Lagace L. Conserved mode of peptidomimetic inhibition and substrate recognition of human cytomegalovirus protease. Nat Struct Biol. 1998 Sep;5(9):819-26. PMID:9731777 doi:10.1038/1860
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