7xtd: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='7xtd' size='340' side='right'caption='[[7xtd]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
<StructureSection load='7xtd' size='340' side='right'caption='[[7xtd]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7xtd]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Komagataella_phaffii Komagataella phaffii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XTD FirstGlance]. <br>
<table><tr><td colspan='2'>[[7xtd]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Komagataella_phaffii Komagataella phaffii] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XTD FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9&#8491;</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=7xtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xtd OCA], [https://pdbe.org/7xtd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xtd RCSB], [https://www.ebi.ac.uk/pdbsum/7xtd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xtd 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=7xtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xtd OCA], [https://pdbe.org/7xtd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xtd RCSB], [https://www.ebi.ac.uk/pdbsum/7xtd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xtd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/C4R4Y0_KOMPG C4R4Y0_KOMPG] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU004279]
[https://www.uniprot.org/uniprot/C4R3K1_KOMPG C4R3K1_KOMPG]  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
During gene transcription, RNA polymerase II (RNAPII) traverses nucleosomes in chromatin, but its mechanism has remained elusive. Using cryo-electron microscopy, we obtained structures of the RNAPII elongation complex (EC) passing through a nucleosome, in the presence of transcription elongation factors Spt6, Spn1, Elf1, Spt4/5, and Paf1C and the histone chaperone FACT. The structures show snapshots of EC progression on DNA, mediating downstream nucleosome disassembly followed by its reassembly upstream of the EC, facilitated by FACT. FACT dynamically adapts to successively occurring subnucleosome intermediates, forming an interface with the EC. Spt6, Spt4/5, and Paf1C form a "cradle" at the EC DNA-exit site, and support the upstream nucleosome reassembly. These structures explain the mechanism by which the EC traverses nucleosomes while maintaining the chromatin structure and epigenetic information.
During gene transcription, RNA polymerase II (RNAPII) traverses nucleosomes in chromatin, but the mechanism has remained elusive. Using cryo-electron microscopy, we obtained structures of the RNAPII elongation complex (EC) passing through a nucleosome in the presence of the transcription elongation factors Spt6, Spn1, Elf1, Spt4/5, and Paf1C and the histone chaperone FACT (facilitates chromatin transcription). The structures show snapshots of EC progression on DNA mediating downstream nucleosome disassembly, followed by its reassembly upstream of the EC, which is facilitated by FACT. FACT dynamically adapts to successively occurring subnucleosome intermediates, forming an interface with the EC. Spt6, Spt4/5, and Paf1C form a "cradle" at the EC DNA-exit site and support the upstream nucleosome reassembly. These structures explain the mechanism by which the EC traverses nucleosomes while maintaining the chromatin structure and epigenetic information.


Structural basis of nucleosome disassembly and reassembly by RNAPII elongation complex with FACT.,Ehara H, Kujirai T, Shirouzu M, Kurumizaka H, Sekine SI Science. 2022 Aug 18:eabp9466. doi: 10.1126/science.abp9466. PMID:35981082<ref>PMID:35981082</ref>
Structural basis of nucleosome disassembly and reassembly by RNAPII elongation complex with FACT.,Ehara H, Kujirai T, Shirouzu M, Kurumizaka H, Sekine SI Science. 2022 Sep 9;377(6611):eabp9466. doi: 10.1126/science.abp9466. Epub 2022 , Aug 18. PMID:35981082<ref>PMID:35981082</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 7xtd" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 7xtd" style="background-color:#fffaf0;"></div>
==See Also==
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Komagataella phaffii]]
[[Category: Komagataella phaffii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Ehara H]]
[[Category: Ehara H]]
[[Category: Kujirai T]]
[[Category: Kujirai T]]

Latest revision as of 10:29, 3 July 2024

RNA polymerase II elongation complex transcribing a nucleosome (EC58oct)RNA polymerase II elongation complex transcribing a nucleosome (EC58oct)

Structural highlights

7xtd is a 12 chain structure with sequence from Homo sapiens, Komagataella phaffii and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C4R3K1_KOMPG

Publication Abstract from PubMed

During gene transcription, RNA polymerase II (RNAPII) traverses nucleosomes in chromatin, but the mechanism has remained elusive. Using cryo-electron microscopy, we obtained structures of the RNAPII elongation complex (EC) passing through a nucleosome in the presence of the transcription elongation factors Spt6, Spn1, Elf1, Spt4/5, and Paf1C and the histone chaperone FACT (facilitates chromatin transcription). The structures show snapshots of EC progression on DNA mediating downstream nucleosome disassembly, followed by its reassembly upstream of the EC, which is facilitated by FACT. FACT dynamically adapts to successively occurring subnucleosome intermediates, forming an interface with the EC. Spt6, Spt4/5, and Paf1C form a "cradle" at the EC DNA-exit site and support the upstream nucleosome reassembly. These structures explain the mechanism by which the EC traverses nucleosomes while maintaining the chromatin structure and epigenetic information.

Structural basis of nucleosome disassembly and reassembly by RNAPII elongation complex with FACT.,Ehara H, Kujirai T, Shirouzu M, Kurumizaka H, Sekine SI Science. 2022 Sep 9;377(6611):eabp9466. doi: 10.1126/science.abp9466. Epub 2022 , Aug 18. PMID:35981082[1]

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

See Also

References

  1. Ehara H, Kujirai T, Shirouzu M, Kurumizaka H, Sekine SI. Structural basis of nucleosome disassembly and reassembly by RNAPII elongation complex with FACT. Science. 2022 Aug 18:eabp9466. doi: 10.1126/science.abp9466. PMID:35981082 doi:http://dx.doi.org/10.1126/science.abp9466

7xtd, resolution 3.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA