5voi: Difference between revisions

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<StructureSection load='5voi' size='340' side='right'caption='[[5voi]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='5voi' size='340' side='right'caption='[[5voi]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5voi]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2] and [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VOI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VOI FirstGlance]. <br>
<table><tr><td colspan='2'>[[5voi]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis], [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27] and [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VOI 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=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]] 2.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vo8|5vo8]]</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='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=5voi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5voi OCA], [https://pdbe.org/5voi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5voi RCSB], [https://www.ebi.ac.uk/pdbsum/5voi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5voi 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=5voi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5voi OCA], [http://pdbe.org/5voi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5voi RCSB], [http://www.ebi.ac.uk/pdbsum/5voi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5voi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RPOZ_THET8 RPOZ_THET8]] Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity). [[http://www.uniprot.org/uniprot/RPOA_THET2 RPOA_THET2]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[http://www.uniprot.org/uniprot/RPOC_THET8 RPOC_THET8]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[http://www.uniprot.org/uniprot/RPOB_THET8 RPOB_THET8]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[http://www.uniprot.org/uniprot/Q5SKW1_THET8 Q5SKW1_THET8]] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released (By similarity).[RuleBase:RU000715]  Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth (By similarity).[HAMAP-Rule:MF_00963]
[https://www.uniprot.org/uniprot/RPOA_THET8 RPOA_THET8] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[RNA polymerase|RNA polymerase]]
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
*[[Sigma factor|Sigma factor]]
*[[Sigma factor 3D structures|Sigma factor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: DNA-directed RNA polymerase]]
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Thet2]]
[[Category: Thermus thermophilus HB27]]
[[Category: Thet8]]
[[Category: Thermus thermophilus HB8]]
[[Category: Jr, C L.Turnbough]]
[[Category: Molodtsov V]]
[[Category: Molodtsov, V]]
[[Category: Murakami KS]]
[[Category: Murakami, K S]]
[[Category: Shin Y]]
[[Category: Shin, Y]]
[[Category: Turnbough Jr CL]]
[[Category: Holoenzyme]]
[[Category: Reiterative transcription]]
[[Category: Rna polymerase]]
[[Category: Thermus thermophilus]]
[[Category: Transcription-dna-rna complex]]

Latest revision as of 16:53, 4 October 2023

X-ray crystal structure of bacterial RNA polymerase and pyrG promoter complexX-ray crystal structure of bacterial RNA polymerase and pyrG promoter complex

Structural highlights

5voi is a 8 chain structure with sequence from Bacillus subtilis, Thermus thermophilus HB27 and Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPOA_THET8 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

Publication Abstract from PubMed

Reiterative transcription is a noncanonical form of RNA synthesis in which a nucleotide specified by a single base in the DNA template is repetitively added to the nascent transcript. Here we determined the crystal structure of an RNA polymerase, the bacterial enzyme from Thermus thermophilus, engaged in reiterative transcription during transcription initiation at a promoter resembling the pyrG promoter of Bacillus subtilis The structure reveals that the reiterative transcript detours from the dedicated RNA exit channel and extends toward the main channel of the enzyme, thereby allowing RNA extension without displacement of the promoter recognition sigma-factor. Nascent transcripts containing reiteratively added G residues are eventually extended by nonreiterative transcription, revealing an atypical pathway for the formation of a transcription elongation complex.

X-ray crystal structure of a reiterative transcription complex reveals an atypical RNA extension pathway.,Murakami KS, Shin Y, Turnbough CL Jr, Molodtsov V Proc Natl Acad Sci U S A. 2017 Aug 1;114(31):8211-8216. doi:, 10.1073/pnas.1702741114. Epub 2017 Jun 26. PMID:28652344[1]

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

See Also

References

  1. Murakami KS, Shin Y, Turnbough CL Jr, Molodtsov V. X-ray crystal structure of a reiterative transcription complex reveals an atypical RNA extension pathway. Proc Natl Acad Sci U S A. 2017 Aug 1;114(31):8211-8216. doi:, 10.1073/pnas.1702741114. Epub 2017 Jun 26. PMID:28652344 doi:http://dx.doi.org/10.1073/pnas.1702741114

5voi, resolution 2.80Å

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