5vi8

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==Structure of a mycobacterium smegmatis transcription initiation complex with an upstream-fork promoter fragment==
==Structure of a mycobacterium smegmatis transcription initiation complex with an upstream-fork promoter fragment==
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<StructureSection load='5vi8' size='340' side='right' caption='[[5vi8]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
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<StructureSection load='5vi8' size='340' side='right'caption='[[5vi8]], [[Resolution|resolution]] 2.76&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5vi8]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VI8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VI8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5vi8]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155] 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=5VI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VI8 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">X-ray diffraction, [[Resolution|Resolution]] 2.76&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rbpA, MSMEG_3858, MSMEI_3768 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2]), rpoD, sigA, MSMEG_2758, MSMEI_2690 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5vi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vi8 OCA], [https://pdbe.org/5vi8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vi8 RCSB], [https://www.ebi.ac.uk/pdbsum/5vi8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vi8 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=5vi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vi8 OCA], [http://pdbe.org/5vi8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vi8 RCSB], [http://www.ebi.ac.uk/pdbsum/5vi8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vi8 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/A0QW02_MYCS2 A0QW02_MYCS2]] 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.[SAAS:SAAS00535554] [[http://www.uniprot.org/uniprot/RPOB_MYCS2 RPOB_MYCS2]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit often mutates to generate rifampicin (Rif) resistance. Interaction with RbpA partially restores Rif-inhibited transcription; once the subunit is Rif-resistant however RbpA no longer stimulates transcription.[HAMAP-Rule:MF_01321]<ref>PMID:19926651</ref> [[http://www.uniprot.org/uniprot/RPOA_MYCS2 RPOA_MYCS2]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00059]<ref>PMID:19926651</ref> [[http://www.uniprot.org/uniprot/RBPA_MYCS2 RBPA_MYCS2]] Binds to RNA polymerase (RNAP), probably stimulating transcriptions from principal, but not alternative sigma factor promoters (By similarity). Partially restores transcription in the presence of rifampicin (Rif) in vitro; overexpression leads to an increase in the Rif tolerance in vivo, with smaller colonies. Seems to act by removing Rif from its binding site and preventing its further binding. No longer stimulates transcription in Rif-resistant RNA polymerase (with mutations in rpoB).<ref>PMID:19926651</ref> <ref>PMID:21415119</ref> [[http://www.uniprot.org/uniprot/RPOC_MYCS2 RPOC_MYCS2]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01322]<ref>PMID:19926651</ref> [[http://www.uniprot.org/uniprot/RPOZ_MYCS2 RPOZ_MYCS2]] 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]<ref>PMID:19926651</ref>
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[https://www.uniprot.org/uniprot/RBPA_MYCS2 RBPA_MYCS2] Binds to RNA polymerase (RNAP), probably stimulating transcriptions from principal, but not alternative sigma factor promoters (By similarity). Partially restores transcription in the presence of rifampicin (Rif) in vitro; overexpression leads to an increase in the Rif tolerance in vivo, with smaller colonies. Seems to act by removing Rif from its binding site and preventing its further binding. No longer stimulates transcription in Rif-resistant RNA polymerase (with mutations in rpoB).<ref>PMID:19926651</ref> <ref>PMID:21415119</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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RbpA and CarD are essential transcription regulators in mycobacteria. Mechanistic analyses of promoter open complex (RPo) formation establish thatRbpA and CarD cooperatively stimulate formation of anintermediate (RP2) leading to RPo; formation of RP2 islikely a bottleneck step at the majority of mycobacterial promoters. Once RPo forms, CarD also disfavors its isomerization back to RP2.We determined a 2.76 A-resolution crystal structure of a mycobacterial transcription initiation complex (TIC) with RbpA as well as a CarD/RbpA/TIC model. Both CarD and RbpA bind near the upstream edge of the -10 element where they likely facilitate DNA bending and impede transcription bubble collapse. In vivo studies demonstrate the essential role of RbpA, effects of RbpA truncations on transcription and cell physiology, and indicate additional functions for RbpA not evident in vitro. This work provides a framework to understand the control of mycobacterial transcriptionby RbpA and CarD.
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The mycobacteria RNA polymerase (RNAP) is a target for antimicrobials against tuberculosis, motivating structure/function studies. Here we report a 3.2 A-resolution crystal structure of a Mycobacterium smegmatis (Msm) open promoter complex (RPo), along with structural analysis of the Msm RPo and a previously reported 2.76 A-resolution crystal structure of an Msm transcription initiation complex with a promoter DNA fragment. We observe the interaction of the Msm RNAP alpha-subunit C-terminal domain (alphaCTD) with DNA, and we provide evidence that the alphaCTD may play a role in Mtb transcription regulation. Our results reveal the structure of an Actinobacteria-unique insert of the RNAP beta' subunit. Finally, our analysis reveals the disposition of the N-terminal segment of Msm sigmaA, which may comprise an intrinsically disordered protein domain unique to mycobacteria. The clade-specific features of the mycobacteria RNAP provide clues to the profound instability of mycobacteria RPo compared with E. coli.
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Structure and function of the mycobacterial transcription initiation complex with the essential regulator RbpA.,Hubin EA, Fay A, Xu C, Bean JM, Saecker RM, Glickman MS, Darst SA, Campbell EA Elife. 2017 Jan 9;6. pii: e22520. doi: 10.7554/eLife.22520. PMID:28067618<ref>PMID:28067618</ref>
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Structural insights into the mycobacteria transcription initiation complex from analysis of X-ray crystal structures.,Hubin EA, Lilic M, Darst SA, Campbell EA Nat Commun. 2017 Jul 13;8:16072. doi: 10.1038/ncomms16072. PMID:28703128<ref>PMID:28703128</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>
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</div>
<div class="pdbe-citations 5vi8" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5vi8" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Sigma factor 3D structures|Sigma factor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: DNA-directed RNA polymerase]]
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[[Category: Large Structures]]
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[[Category: Mycs2]]
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[[Category: Mycolicibacterium smegmatis MC2 155]]
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[[Category: Campbell, E A]]
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[[Category: Synthetic construct]]
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[[Category: Darst, S A]]
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[[Category: Campbell EA]]
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[[Category: Hubin, E A]]
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[[Category: Darst SA]]
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[[Category: Dna-dependent rna polymerase]]
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[[Category: Hubin EA]]
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[[Category: Nucleotidyl transferase]]
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[[Category: Transcription]]
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[[Category: Transcription initiation complex]]
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Current revision

Structure of a mycobacterium smegmatis transcription initiation complex with an upstream-fork promoter fragment

PDB ID 5vi8

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