6ogy

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<SX load='6ogy' size='340' side='right' viewer='molstar' caption='[[6ogy]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<SX load='6ogy' size='340' side='right' viewer='molstar' caption='[[6ogy]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ogy]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/Rotavirus_a Rotavirus a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OGY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OGY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ogy]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Rotavirus_A Rotavirus A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OGY FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTG:7-METHYL-GUANOSINE-5-TRIPHOSPHATE-5-GUANOSINE'>GTG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTG:7-METHYL-GUANOSINE-5-TRIPHOSPHATE-5-GUANOSINE'>GTG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ogy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ogy OCA], [http://pdbe.org/6ogy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ogy RCSB], [http://www.ebi.ac.uk/pdbsum/6ogy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ogy ProSAT]</span></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=6ogy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ogy OCA], [https://pdbe.org/6ogy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ogy RCSB], [https://www.ebi.ac.uk/pdbsum/6ogy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ogy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/G0YZJ9_9REOV G0YZJ9_9REOV]] RNA-directed RNA polymerase that is involved in both transcription and genome replication. Together with VP3 capping enzyme, forms an enzyme complex positioned near the channels situated at each of the five-fold vertices of the core. Following infection, the outermost layer of the virus is lost, leaving a double-layered particle (DLP) made up of the core and VP6 shell. VP1 then catalyzes the transcription of fully conservative plus-strand genomic RNAs that are extruded through the DLP's channels into the cytoplasm where they function as mRNAs for translation of viral proteins. One copy of each of the viral (+)RNAs is also recruited during core assembly, together with newly synthesized polymerase complexes and VP2. The polymerase of these novo-formed particles catalyzes the synthesis of complementary minus-strands leading to dsRNA formation. To do so, the polymerase specifically recognizes and binds 4 bases 5'-UGUG-3' in the conserved 3'-sequence of plus-strand RNA templates. VP2 presumably activates the autoinhibited VP1-RNA complex to coordinate packaging and genome replication. Once dsRNA synthesis is complete, the polymerase switches to the transcriptional mode, thus providing secondary transcription.[RuleBase:RU363117] [[http://www.uniprot.org/uniprot/G0YZK0_9REOV G0YZK0_9REOV]] Inner capsid protein that self-assembles to form an icosahedral capsid with a T=2 symmetry, which consists of 120 copies of VP2, with channels at each of its five-fold vertices. This capsid constitutes the innermost concentric layer of the viral mature particle. It encapsidates the polymerase VP1, the capping enzyme VP3 and the genomic dsRNA, thereby defining the core. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels formed by VP2 N-termini. VP2 is required for the replicase activity of VP1 polymerase. Probably recruits a copy of a VP1-VP3 complex, potentially along with a segment of plus-strand RNA, as a decamer of VP2 assembles. May activate the autoinhibited VP1/RNA complex to coordinate packaging and genome replication.[RuleBase:RU363125]
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[https://www.uniprot.org/uniprot/G0YZJ9_9VIRU G0YZJ9_9VIRU]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Transcribing and replicating a double-stranded genome require protein modules to unwind, transcribe/replicate nucleic acid substrates, and release products. Here we present in situ cryo-electron microscopy structures of rotavirus dsRNA-dependent RNA polymerase (RdRp) in two states pertaining to transcription. In addition to the previously discovered universal "hand-shaped" polymerase core domain shared by DNA polymerases and telomerases, our results show the function of N- and C-terminal domains of RdRp: the former opens the genome duplex to isolate the template strand; the latter splits the emerging template-transcript hybrid, guides genome reannealing to form a transcription bubble, and opens a capsid shell protein (CSP) to release the transcript. These two "helicase" domains also extensively interact with CSP, which has a switchable N-terminal helix that, like cellular transcriptional factors, either inhibits or promotes RdRp activity. The in situ structures of RdRp, CSP, and RNA in action inform mechanisms of not only transcription, but also replication.
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In situ structures of rotavirus polymerase in action and mechanism of mRNA transcription and release.,Ding K, Celma CC, Zhang X, Chang T, Shen W, Atanasov I, Roy P, Zhou ZH Nat Commun. 2019 May 17;10(1):2216. doi: 10.1038/s41467-019-10236-7. PMID:31101900<ref>PMID:31101900</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 6ogy" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
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== References ==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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<references/>
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__TOC__
__TOC__
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: RNA-directed RNA polymerase]]
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[[Category: Rotavirus A]]
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[[Category: Rotavirus a]]
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[[Category: Chang T]]
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[[Category: Chang, T]]
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[[Category: Ding K]]
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[[Category: Ding, K]]
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[[Category: Roy P]]
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[[Category: Roy, P]]
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[[Category: Shen W]]
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[[Category: Shen, W]]
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[[Category: Zhou ZH]]
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[[Category: Zhou, Z H]]
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[[Category: Capsid shell protein]]
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[[Category: In situ structure]]
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[[Category: Reovirus]]
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[[Category: Rna-dependent rna polymerase]]
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[[Category: Rotavirus]]
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[[Category: Transcription]]
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[[Category: Transcriptional factor]]
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[[Category: Viral protein-transferase-rna complex]]
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[[Category: Virus]]
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Current revision

In situ structure of Rotavirus RNA-dependent RNA polymerase at duplex-open state

6ogy, resolution 3.40Å

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