7e6v

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<StructureSection load='7e6v' size='340' side='right'caption='[[7e6v]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
<StructureSection load='7e6v' size='340' side='right'caption='[[7e6v]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7e6v]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E6V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7e6v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus_SAT_2 Foot-and-mouth disease virus SAT 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E6V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e6v OCA], [https://pdbe.org/7e6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e6v RCSB], [https://www.ebi.ac.uk/pdbsum/7e6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e6v ProSAT]</span></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=7e6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e6v OCA], [https://pdbe.org/7e6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e6v RCSB], [https://www.ebi.ac.uk/pdbsum/7e6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e6v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/B8Y0J7_9PICO B8Y0J7_9PICO]] Associates with and induces structural rearrangements of intracellular membranes. Triggers host autophagy by interacting with host BECN1 and thereby promotes viral replication. Participates in viral replication and interacts with host DHX9. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.[ARBA:ARBA00003578] Capsid protein V3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3. The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome.[ARBA:ARBA00003160] Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.[ARBA:ARBA00002573] Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, binds to viral RNA and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease.[ARBA:ARBA00004047] Mediates self-processing of the polyprotein by a translational effect termed 'ribosome skipping'. Mechanistically, 2A-mediated cleavage occurs between the C-terminal glycine and the proline of the downstream protein 2B. In the case of foot-and-mouth disease virus, the 2A oligopeptide is post-translationally 'trimmed' from the C-terminus of the upstream protein 1D by 3C proteinase.[ARBA:ARBA00002616] Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.[ARBA:ARBA00003379] Plays important roles in virus replication, virulence and host range.[ARBA:ARBA00003095] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated.[ARBA:ARBA00004027]
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[[https://www.uniprot.org/uniprot/B8Y0J7_9PICO B8Y0J7_9PICO]] Associates with and induces structural rearrangements of intracellular membranes. Triggers host autophagy by interacting with host BECN1 and thereby promotes viral replication. Participates in viral replication and interacts with host DHX9. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.[ARBA:ARBA00003578] Capsid protein V3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3. The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome.[ARBA:ARBA00003160] Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.[ARBA:ARBA00002573] Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, binds to viral RNA and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease.[ARBA:ARBA00004047] Mediates self-processing of the polyprotein by a translational effect termed 'ribosome skipping'. Mechanistically, 2A-mediated cleavage occurs between the C-terminal glycine and the proline of the downstream protein 2B. In the case of foot-and-mouth disease virus, the 2A oligopeptide is post-translationally 'trimmed' from the C-terminus of the upstream protein 1D by 3C proteinase.[ARBA:ARBA00002616] Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.[ARBA:ARBA00003379] Plays important roles in virus replication, virulence and host range.[ARBA:ARBA00003095] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated.[ARBA:ARBA00004027]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The foot-and-mouth disease virus (FMDV) 2C protein shares conserved motifs with enterovirus 2Cs despite low sequence identity. Here, we determine the crystal structure of an FMDV 2C fragment to 1.83 A resolution, which comprises an ATPase domain, a region equivalent to the enterovirus 2C zinc-finger (ZFER), and a C-terminal domain harboring a loop (PBL) that occupies a hydrophobic cleft (Pocket) in an adjacent 2C molecule. Mutations at ZFER, PBL, and Pocket affect FMDV 2C ATPase activity and are lethal to FMDV infectious clones. Because the PBL-Pocket interaction between FMDV 2C molecules is essential for its functions, we design an anti-FMDV peptide derived from PBL (PBL-peptide). PBL-peptide inhibits FMDV 2C ATPase activity, binds FMDV 2C with nanomolar affinity, and disrupts FMDV 2C oligomerization. FMDV 2C targets lipid droplets (LDs) and induces LD clustering in cells, and PBL-peptide disrupts FMDV 2C-induced LD clustering. Finally, we demonstrate that PBL-peptide exhibits anti-FMDV activity in cells.
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An anti-picornaviral strategy based on the crystal structure of foot-and-mouth disease virus 2C protein.,Zhang C, Yang F, Wojdyla JA, Qin B, Zhang W, Zheng M, Cao W, Wang M, Gao X, Zheng H, Cui S Cell Rep. 2022 Jul 5;40(1):111030. doi: 10.1016/j.celrep.2022.111030. PMID:35793627<ref>PMID:35793627</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7e6v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Foot-and-mouth disease virus SAT 2]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cui, S]]
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[[Category: Cui S]]
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[[Category: Gao, X]]
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[[Category: Gao X]]
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[[Category: Qin, B]]
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[[Category: Qin B]]
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[[Category: Wang, M]]
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[[Category: Wang M]]
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[[Category: Wojdyla, J A]]
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[[Category: Wojdyla JA]]
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[[Category: Zhang, C]]
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[[Category: Zhang C]]
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[[Category: Fmdv]]
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[[Category: Hydrolase]]
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Revision as of 05:22, 8 September 2022

The crystal structure of foot-and-mouth disease virus(FMDV) 2C protein 97-318aa

PDB ID 7e6v

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