6c9y

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<SX load='6c9y' size='340' side='right' viewer='molstar' caption='[[6c9y]], [[Resolution|resolution]] 4.25&Aring;' scene=''>
<SX load='6c9y' size='340' side='right' viewer='molstar' caption='[[6c9y]], [[Resolution|resolution]] 4.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6c9y]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C9Y FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6c9y]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C9Y FirstGlance]. <br>
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</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>
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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]] 4.25&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpoA, pez, phs, sez, b3295, JW3257 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), rpoB, groN, nitB, rif, ron, stl, stv, tabD, b3987, JW3950 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), rpoC, tabB, b3988, JW3951 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), rpoZ, b3649, JW3624 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), rpoD, alt, b3067, JW3039 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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/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>
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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=6c9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c9y OCA], [https://pdbe.org/6c9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c9y RCSB], [https://www.ebi.ac.uk/pdbsum/6c9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c9y ProSAT]</span></td></tr>
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<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=6c9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c9y OCA], [http://pdbe.org/6c9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c9y RCSB], [http://www.ebi.ac.uk/pdbsum/6c9y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c9y ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RPOZ_ECOLI RPOZ_ECOLI]] 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.[HAMAP-Rule:MF_00366] [[http://www.uniprot.org/uniprot/RPOA_ECOLI RPOA_ECOLI]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.[HAMAP-Rule:MF_00059] [[http://www.uniprot.org/uniprot/RPOC_ECOLI RPOC_ECOLI]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01322] [[http://www.uniprot.org/uniprot/RPOB_ECOLI RPOB_ECOLI]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01321] [[http://www.uniprot.org/uniprot/RPOD_ECOLI RPOD_ECOLI]] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This is the primary sigma factor of this bacterium.
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[https://www.uniprot.org/uniprot/RPOC_ECOLI RPOC_ECOLI] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01322]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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First step of gene expression is transcribing the genetic information stored in DNA to RNA by the transcription machinery including RNA polymerase (RNAP). In Escherichia coli, a primary sigma70 factor form the RNAP holoenzyme to express housekeeping genes. The sigma70 contains a large insertion at between the conserved regions 1.2 and 2.1, the sigma non-conserved region (sigmaNCR), but its function remains to be elucidated. In this study, we determined the cryo-EM structures of the E. coli RNAP sigma70 holoenzyme and its complex with promoter DNA (open complex, RPo) at 4.2 and 5.75 A resolutions, respectively, to reveal native conformations of RNAP and DNA. The RPo structure presented here found an interaction between R157 residue in the sNCR and promoter DNA just upstream of the -10 element, which was not observed in a previously determined E. coli RNAP transcription initiation complex (RPo plus short RNA) structure by X-ray crystallography due to restraint of crystal packing effect. Disruption of the sNCR and DNA interaction by the amino acid substitutions (R157A/E) influences the DNA opening around the transcription start site and therefore decreases the transcription activity of RNAP. We propose that the sNCR and DNA interaction is conserved in proteobacteria and RNAP in other bacteria replace its role with a transcription factor.
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Cryo-EM structure of Escherichia coli sigma(70) RNAP and promoter DNA complex revealed a role of sigma non-conserved region during the open complex formation.,Narayanan A, Vago FS, Li K, Qayyum MZ, Yernool D, Jiang W, Murakami KS J Biol Chem. 2018 Mar 26. pii: RA118.002161. doi: 10.1074/jbc.RA118.002161. PMID:29581236<ref>PMID:29581236</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 6c9y" 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]]
*[[Sigma factor 3D structures|Sigma factor 3D structures]]
*[[Sigma factor 3D structures|Sigma factor 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</SX>
</SX>
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[[Category: DNA-directed RNA polymerase]]
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[[Category: Escherichia coli K-12]]
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[[Category: Ecoli]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Jiang, W]]
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[[Category: Jiang W]]
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[[Category: Li, K]]
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[[Category: Li K]]
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[[Category: Murakami, K S]]
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[[Category: Murakami KS]]
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[[Category: Narayanan, A]]
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[[Category: Narayanan A]]
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[[Category: Qayyum, M Z]]
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[[Category: Qayyum MZ]]
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[[Category: Vago, F]]
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[[Category: Vago F]]
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[[Category: Yenool, D]]
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[[Category: Yenool D]]
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[[Category: Escherichia coli]]
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[[Category: Rna polymerase]]
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[[Category: Transcription]]
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Current revision

Cryo-EM structure of E. coli RNAP sigma70 holoenzyme

6c9y, resolution 4.25Å

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