8h56

From Proteopedia

(Difference between revisions)

Revision as of 04:07, 25 May 2023

Crystal structure of Rep' of porcine circovirus type 2

Structural highlights

8h56 is a 2 chain structure with sequence from Porcine circovirus 2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

REP_PCV2 Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep and/or Rep' binds a specific hairpin at the genome origin of replication. Introduces an endonucleolytic nick within the conserved sequence 5'-AGTATTAC-3' in the intergenic region of the genome, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, and nucleotidyl transferase.^[1] ^[2]

Publication Abstract from PubMed

Porcine circovirus type 2 (PCV2) can cause porcine circovirus-associated disease (PCVAD), which causes significant economic losses to the global pig industry annually. There are no effective antiviral drugs used to control and treat PCV2, and prevention is mainly obtained through vaccination. PCV2 genome replicates through the rolling circle replication (RCR) mechanism involving Rep and Rep', so analyzing the holistic structure of Rep and Rep' will help us better understand the replication process of PCV2. However, there are no reports on the integral structure of Rep' and Rep, which seriously hinders the research of the viral replication. By using the x-ray diffraction method, the structure of the Rep' dimer was resolved by us in this study. Structural analysis revealed that Rep' is a dimer formed by the interaction of the C-terminal domain. The two Rep' form a positively charged groove, which may play an essential role in the viral binding of dsDNA. Together, this study help to understand the replication process of the virus and may also provide new insights into the development of antiviral drugs.

Crystal structure of the dimerized of porcine circovirus type II replication-related protein Rep'.,Guan S, Tian A, Jing H, Yuan H, Jia H, Shi Y, Chen H, Cao S, Peng G, Song Y Proteins. 2023 May 12. doi: 10.1002/prot.26498. PMID:37171131^[3]

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

References

↑ Cheung AK. The essential and nonessential transcription units for viral protein synthesis and DNA replication of porcine circovirus type 2. Virology. 2003 Sep 1;313(2):452-9. PMID:12954212 doi:10.1016/s0042-6822(03)00373-8
↑ Cheung AK. Specific functions of the Rep and Rep׳ proteins of porcine circovirus during copy-release and rolling-circle DNA replication. Virology. 2015 Jul;481:43-50. PMID:25768890 doi:10.1016/j.virol.2015.01.004
↑ Guan S, Tian A, Jing H, Yuan H, Jia H, Shi Y, Chen H, Cao S, Peng G, Song Y. Crystal structure of the dimerized of porcine circovirus type II replication-related protein Rep'. Proteins. 2023 May 12. PMID:37171131 doi:10.1002/prot.26498

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8h56"

Categories: Large Structures | Porcine circovirus 2 | Guan SY | Song YF

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8h56 is ON HOLD  until Paper Publication
+==Crystal structure of Rep' of porcine circovirus type 2==
+<StructureSection load='8h56' size='340' side='right'caption='[[8h56]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8h56]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Porcine_circovirus_2 Porcine circovirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8H56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H56 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=8h56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h56 OCA], [https://pdbe.org/8h56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h56 RCSB], [https://www.ebi.ac.uk/pdbsum/8h56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h56 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/REP_PCV2 REP_PCV2] Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep and/or Rep' binds a specific hairpin at the genome origin of replication. Introduces an endonucleolytic nick within the conserved sequence 5'-AGTATTAC-3' in the intergenic region of the genome, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, and nucleotidyl transferase.<ref>PMID:12954212</ref> <ref>PMID:25768890</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Porcine circovirus type 2 (PCV2) can cause porcine circovirus-associated disease (PCVAD), which causes significant economic losses to the global pig industry annually. There are no effective antiviral drugs used to control and treat PCV2, and prevention is mainly obtained through vaccination. PCV2 genome replicates through the rolling circle replication (RCR) mechanism involving Rep and Rep', so analyzing the holistic structure of Rep and Rep' will help us better understand the replication process of PCV2. However, there are no reports on the integral structure of Rep' and Rep, which seriously hinders the research of the viral replication. By using the x-ray diffraction method, the structure of the Rep' dimer was resolved by us in this study. Structural analysis revealed that Rep' is a dimer formed by the interaction of the C-terminal domain. The two Rep' form a positively charged groove, which may play an essential role in the viral binding of dsDNA. Together, this study help to understand the replication process of the virus and may also provide new insights into the development of antiviral drugs.
-Authors:
+Crystal structure of the dimerized of porcine circovirus type II replication-related protein Rep'.,Guan S, Tian A, Jing H, Yuan H, Jia H, Shi Y, Chen H, Cao S, Peng G, Song Y Proteins. 2023 May 12. doi: 10.1002/prot.26498. PMID:37171131<ref>PMID:37171131</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8h56" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Porcine circovirus 2]]
+[[Category: Guan SY]]
+[[Category: Song YF]]

8h56

From Proteopedia

Revision as of 04:07, 25 May 2023

Crystal structure of Rep' of porcine circovirus type 2

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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