4egt: Difference between revisions

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'''Unreleased structure'''


The entry 4egt is ON HOLD until Paper Publication
==Crystal structure of major capsid protein P domain from rabbit hemorrhagic disease virus==
<StructureSection load='4egt' size='340' side='right'caption='[[4egt]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4egt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rabbit_hemorrhagic_disease_virus Rabbit hemorrhagic disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EGT 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]] 2&#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=4egt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4egt OCA], [https://pdbe.org/4egt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4egt RCSB], [https://www.ebi.ac.uk/pdbsum/4egt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4egt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q3HNQ2_RHDV Q3HNQ2_RHDV] 3C-like protease processes the polyprotein: 3CLpro-RdRp (p72) is first released by autocleavage, then all other proteins are cleaved.[ARBA:ARBA00003176] Capsid protein VP60 self assembles to form an icosahedral capsid with a T=3 symmetry, about 35 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate VP2 proteins and genomic or subgenomic RNA. Attaches virion to target cells by binding histo-blood group antigens, inducing endocytosis of the viral particle. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm.[ARBA:ARBA00024666]  NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.[ARBA:ARBA00025124]  Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation.[ARBA:ARBA00025359]


Authors: Wang, X., Xu, F., Zhang, K., Zhai, Y., Sun, F.
==See Also==
 
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
Description: Crystal structure of major capsid protein P domain from rabbit hemorrhagic disease virus
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rabbit hemorrhagic disease virus]]
[[Category: Sun F]]
[[Category: Wang X]]
[[Category: Xu F]]
[[Category: Zhai Y]]
[[Category: Zhang K]]

Latest revision as of 18:01, 14 March 2024

Crystal structure of major capsid protein P domain from rabbit hemorrhagic disease virusCrystal structure of major capsid protein P domain from rabbit hemorrhagic disease virus

Structural highlights

4egt is a 2 chain structure with sequence from Rabbit hemorrhagic disease virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q3HNQ2_RHDV 3C-like protease processes the polyprotein: 3CLpro-RdRp (p72) is first released by autocleavage, then all other proteins are cleaved.[ARBA:ARBA00003176] Capsid protein VP60 self assembles to form an icosahedral capsid with a T=3 symmetry, about 35 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate VP2 proteins and genomic or subgenomic RNA. Attaches virion to target cells by binding histo-blood group antigens, inducing endocytosis of the viral particle. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm.[ARBA:ARBA00024666] NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.[ARBA:ARBA00025124] Viral genome-linked protein is covalently linked to the 5'-end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation.[ARBA:ARBA00025359]

See Also

4egt, resolution 2.00Å

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