4v8s: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
==Archaeal RNAP-DNA binary complex at 4.32Ang==
==Archaeal RNAP-DNA binary complex at 4.32Ang==
<StructureSection load='4v8s' size='340' side='right' caption='[[4v8s]], [[Resolution|resolution]] 4.32&Aring;' scene=''>
<StructureSection load='4v8s' size='340' side='right'caption='[[4v8s]], [[Resolution|resolution]] 4.32&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4v8s]] is a 30 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfolobus_shibatae_b12 Sulfolobus shibatae b12]. This structure supersedes and combines the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4b1o 4b1o] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4b1p 4b1p]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V8S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V8S FirstGlance]. <br>
<table><tr><td colspan='2'>[[4v8s]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_shibatae_B12 Saccharolobus shibatae B12] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4b1o 4b1o] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4b1p 4b1p]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V8S FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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">X-ray diffraction, [[Resolution|Resolution]] 4.323&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b1o|4b1o]], [[4b1p|4b1p]], [[2y0s|2y0s]], [[4ayb|4ayb]]</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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </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=4v8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v8s OCA], [https://pdbe.org/4v8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v8s RCSB], [https://www.ebi.ac.uk/pdbsum/4v8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v8s ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4v8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v8s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v8s RCSB], [http://www.ebi.ac.uk/pdbsum/4v8s PDBsum]</span></td></tr>
</table>
</table>
{{Large structure}}
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/B8YB63_SULSH B8YB63_SULSH]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00250] [[http://www.uniprot.org/uniprot/B8YB61_SULSH B8YB61_SULSH]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00192] [[http://www.uniprot.org/uniprot/B8YB60_SULSH B8YB60_SULSH]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00025] [[http://www.uniprot.org/uniprot/B8YB54_SULSH B8YB54_SULSH]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00411] [[http://www.uniprot.org/uniprot/B8YB56_SULSH B8YB56_SULSH]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00320] [[http://www.uniprot.org/uniprot/B8YB64_SULSH B8YB64_SULSH]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00615] [[http://www.uniprot.org/uniprot/B8YB62_SULSH B8YB62_SULSH]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).[HAMAP-Rule:MF_00261]  
[https://www.uniprot.org/uniprot/RPO6_SACSH RPO6_SACSH] DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00192]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 19: Line 18:
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 4v8s" style="background-color:#fffaf0;"></div>
==See Also==
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: DNA-directed RNA polymerase]]
[[Category: Large Structures]]
[[Category: Sulfolobus shibatae b12]]
[[Category: Saccharolobus shibatae B12]]
[[Category: Abrescia, N G.A]]
[[Category: Synthetic construct]]
[[Category: Bell, S D]]
[[Category: Abrescia NGA]]
[[Category: Millet, O]]
[[Category: Bell SD]]
[[Category: Mogni, M]]
[[Category: Millet O]]
[[Category: Wojtas, M N]]
[[Category: Mogni M]]
[[Category: Transcription]]
[[Category: Wojtas MN]]
[[Category: Transferase-dna complex]]

Latest revision as of 13:40, 10 January 2024

Archaeal RNAP-DNA binary complex at 4.32AngArchaeal RNAP-DNA binary complex at 4.32Ang

Structural highlights

4v8s is a 20 chain structure with sequence from Saccharolobus shibatae B12 and Synthetic construct. This structure supersedes the now removed PDB entries 4b1o and 4b1p. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 4.323Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPO6_SACSH DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00192]

Publication Abstract from PubMed

Multi-subunit RNA polymerases (RNAPs) in all three domains of life share a common ancestry. The composition of the archaeal RNAP (aRNAP) is not identical between phyla and species, with subunits Rpo8 and Rpo13 found in restricted subsets of archaea. While Rpo8 has an ortholog, Rpb8, in the nuclear eukaryal RNAPs, Rpo13 lacks clear eukaryal orthologs. Here, we report crystal structures of the DNA-bound and free form of the aRNAP from Sulfolobus shibatae. Together with biochemical and biophysical analyses, these data show that Rpo13 C-terminus binds non-specifically to double-stranded DNA. These interactions map on our RNAP-DNA binary complex on the downstream DNA at the far end of the DNA entry channel. Our findings thus support Rpo13 as a RNAP-DNA stabilization factor, a role reminiscent of eukaryotic general transcriptional factors. The data further yield insight into the mechanisms and evolution of RNAP-DNA interaction.

Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA.,Wojtas MN, Mogni M, Millet O, Bell SD, Abrescia NG Nucleic Acids Res. 2012 Jul 30. PMID:22848102[1]

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

See Also

References

  1. Wojtas MN, Mogni M, Millet O, Bell SD, Abrescia NG. Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA. Nucleic Acids Res. 2012 Jul 30. PMID:22848102 doi:10.1093/nar/gks692

4v8s, resolution 4.32Å

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