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| <SX load='6eec' size='340' side='right' viewer='molstar' caption='[[6eec]], [[Resolution|resolution]] 3.55Å' scene=''> | | <SX load='6eec' size='340' side='right' viewer='molstar' caption='[[6eec]], [[Resolution|resolution]] 3.55Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6eec]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EEC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6EEC FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6eec]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EEC FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C0L:methyl+[(1E,5R)-5-{(3E)-3-[(2E,4E,8R,9E,12E)-1,8-dihydroxy-2,5,9-trimethyltetradeca-2,4,9,12-tetraen-1-ylidene]-2,4-dioxo-3,4-dihydro-2H-pyran-6-yl}hex-1-en-1-yl]carbamate'>C0L</scene>, <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]] 3.55Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpoA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884]), rpoB, SAMEA2682864_01701 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884]), rpoC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884]), rpoZ, ERS007672_03979, ERS007703_04032, ERS007720_04749, ERS027652_00548, ERS027654_02543, ERS027656_03959, ERS124361_02246 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884]), sigA, mysA, rpoD, rpoV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884]), rbpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884]), carD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C0L:methyl+[(1E,5R)-5-{(3E)-3-[(2E,4E,8R,9E,12E)-1,8-dihydroxy-2,5,9-trimethyltetradeca-2,4,9,12-tetraen-1-ylidene]-2,4-dioxo-3,4-d+ihydro-2H-pyran-6-yl}hex-1-en-1-yl]carbamate'>C0L</scene>, <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=6eec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eec OCA], [https://pdbe.org/6eec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eec RCSB], [https://www.ebi.ac.uk/pdbsum/6eec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eec ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6eec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eec OCA], [http://pdbe.org/6eec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eec RCSB], [http://www.ebi.ac.uk/pdbsum/6eec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eec ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/RBPA_MYCTO RBPA_MYCTO]] Binds to RNA polymerase (RNAP), stimulating transcription from principal, but not alternative sigma factor promoters. [[http://www.uniprot.org/uniprot/RPOC_MYCTA RPOC_MYCTA]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[http://www.uniprot.org/uniprot/CARD_MYCTO CARD_MYCTO]] Controls rRNA transcription by binding to the RNA polymerase (RNAP). Required for replication and persistence during infection of mice (By similarity). [[http://www.uniprot.org/uniprot/V9Z879_MYCTX V9Z879_MYCTX]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU363031] [[http://www.uniprot.org/uniprot/RPOA_MYCTA RPOA_MYCTA]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[http://www.uniprot.org/uniprot/A0A0T9N9K3_MYCTX A0A0T9N9K3_MYCTX]] 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][SAAS:SAAS00298387] [[http://www.uniprot.org/uniprot/SIGA_MYCTO SIGA_MYCTO]] 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.[HAMAP-Rule:MF_00963] | | [https://www.uniprot.org/uniprot/RBPA_MYCTU RBPA_MYCTU] Binds to RNA polymerase (RNAP), stimulating and stabilizing the formation of stable RNAP promoter complexes up to 2-fold from principal sigma factor SigA-dependent but not alternative sigma factor SigF-dependent promoters. Increases the affinity of core RNAP for SigA, increasing the transcriptional activity of RNAP. Unlike the case in M.smegmatis or S.coelicolor, has no effect on rifampicin inhibition of transcription. Has no effect on E.coli RNAP.<ref>PMID:22570422</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
| |
| A key regulated step of transcription is promoter melting by RNA polymerase (RNAP) to form the open promoter complex(1-3). To generate the open complex, the conserved catalytic core of the RNAP combines with initiation factors to locate promoter DNA, unwind 12-14 base pairs of the DNA duplex and load the template-strand DNA into the RNAP active site. Formation of the open complex is a multi-step process during which transient intermediates of unknown structure are formed(4-6). Here we present cryo-electron microscopy structures of bacterial RNAP-promoter DNA complexes, including structures of partially melted intermediates. The structures show that late steps of promoter melting occur within the RNAP cleft, delineate key roles for fork-loop 2 and switch 2-universal structural features of RNAP-in restricting access of DNA to the RNAP active site, and explain why clamp opening is required to allow entry of single-stranded template DNA into the active site. The key roles of fork-loop 2 and switch 2 suggest a common mechanism for late steps in promoter DNA opening to enable gene expression across all domains of life.
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| Structures of an RNA polymerase promoter melting intermediate elucidate DNA unwinding.,Boyaci H, Chen J, Jansen R, Darst SA, Campbell EA Nature. 2019 Jan;565(7739):382-385. doi: 10.1038/s41586-018-0840-5. Epub 2019 Jan, 9. PMID:30626968<ref>PMID:30626968</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6eec" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
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| __TOC__ | | __TOC__ |
| </SX> | | </SX> |
| [[Category: DNA-directed RNA polymerase]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Campbell, E A]] | | [[Category: Mycobacterium tuberculosis]] |
| [[Category: Chen, J]]
| | [[Category: Boyaci Selcuk H]] |
| [[Category: Darst, S A]]
| | [[Category: Campbell EA]] |
| [[Category: Selcuk, H Boyaci]] | | [[Category: Chen J]] |
| [[Category: Closed clamp]] | | [[Category: Darst SA]] |
| [[Category: Initiation]] | |
| [[Category: Open promoter complex]] | |
| [[Category: Transcription]]
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| [[Category: Transcription bubble]]
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| [[Category: Transcription-dna complex]]
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