7ap8: Difference between revisions
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==== | ==Atomic structure of the poxvirus initially transcribing complex in conformation 2== | ||
<StructureSection load='7ap8' size='340' side='right'caption='[[7ap8]]' scene=''> | <StructureSection load='7ap8' size='340' side='right'caption='[[7ap8]], [[Resolution|resolution]] 3.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ap8]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_GLV-1h68 Vaccinia virus GLV-1h68]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AP8 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=7ap8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ap8 OCA], [https://pdbe.org/7ap8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ap8 RCSB], [https://www.ebi.ac.uk/pdbsum/7ap8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ap8 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.15Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7ap8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ap8 OCA], [https://pdbe.org/7ap8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ap8 RCSB], [https://www.ebi.ac.uk/pdbsum/7ap8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ap8 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q1PIV1_9POXV Q1PIV1_9POXV] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Poxviruses express their genes in the cytoplasm of infected cells using a virus-encoded multi-subunit polymerase (vRNAP) and unique transcription factors. We present cryo-EM structures that uncover the complete transcription initiation phase of the poxvirus vaccinia. In the pre-initiation complex, the heterodimeric early transcription factor VETFs/l adopts an arc-like shape spanning the polymerase cleft and anchoring upstream and downstream promoter elements. VETFI emerges as a TBP-like protein that inserts asymmetrically into the DNA major groove, triggers DNA melting, ensures promoter recognition and enforces transcription directionality. The helicase VETFs fosters promoter melting and the phospho-peptide domain (PPD) of vRNAP subunit Rpo30 enables transcription initiation. An unprecedented upstream promoter scrunching mechanism assisted by the helicase NPH-I probably fosters promoter escape and transition into elongation. Our structures shed light on unique mechanisms of poxviral gene expression and aid the understanding of thus far unexplained universal principles in transcription. | |||
Structural basis of the complete poxvirus transcription initiation process.,Grimm C, Bartuli J, Boettcher B, Szalay AA, Fischer U Nat Struct Mol Biol. 2021 Oct;28(10):779-788. doi: 10.1038/s41594-021-00655-w. , Epub 2021 Sep 23. PMID:34556871<ref>PMID:34556871</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ap8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Vaccinia virus GLV-1h68]] | ||
[[Category: Bartuli J]] | |||
[[Category: Fischer U]] | |||
[[Category: Grimm C]] | |||
Latest revision as of 09:04, 21 November 2024
Atomic structure of the poxvirus initially transcribing complex in conformation 2Atomic structure of the poxvirus initially transcribing complex in conformation 2
Structural highlights
FunctionPublication Abstract from PubMedPoxviruses express their genes in the cytoplasm of infected cells using a virus-encoded multi-subunit polymerase (vRNAP) and unique transcription factors. We present cryo-EM structures that uncover the complete transcription initiation phase of the poxvirus vaccinia. In the pre-initiation complex, the heterodimeric early transcription factor VETFs/l adopts an arc-like shape spanning the polymerase cleft and anchoring upstream and downstream promoter elements. VETFI emerges as a TBP-like protein that inserts asymmetrically into the DNA major groove, triggers DNA melting, ensures promoter recognition and enforces transcription directionality. The helicase VETFs fosters promoter melting and the phospho-peptide domain (PPD) of vRNAP subunit Rpo30 enables transcription initiation. An unprecedented upstream promoter scrunching mechanism assisted by the helicase NPH-I probably fosters promoter escape and transition into elongation. Our structures shed light on unique mechanisms of poxviral gene expression and aid the understanding of thus far unexplained universal principles in transcription. Structural basis of the complete poxvirus transcription initiation process.,Grimm C, Bartuli J, Boettcher B, Szalay AA, Fischer U Nat Struct Mol Biol. 2021 Oct;28(10):779-788. doi: 10.1038/s41594-021-00655-w. , Epub 2021 Sep 23. PMID:34556871[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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