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6dve

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Current revision

Crystal structure of Mycobacterium tuberculosis transcription initiation complex(ECF selenomethionine-labelled sigma factor L) with 6 nt spacer

Structural highlights

6dve is a 8 chain structure with sequence from Myctu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Gene:	rpoA, Rv3457c, MTCY13E12.10c (MYCTU), rpoB, Rv0667, MTCI376.08c (MYCTU), rpoC, Rv0668, MTCI376.07c (MYCTU), rpoZ, Rv1390, MTCY21B4.07 (MYCTU), sigL, Rv0735 (MYCTU)
Activity:	DNA-directed RNA polymerase, with EC number 2.7.7.6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RPOZ_MYCTU] 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.^[1] [RPOA_MYCTU] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00059]^[2] [RPOC_MYCTU] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01322]^[3] [RPOB_MYCTU] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01321] [SIGL_MYCTU] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis. Over-expression of SigL induces 19-28 genes including polyketide synthases, secreted and membrane proteins. Might play a minor role in regulating SigB.^[4] ^[5]

Publication Abstract from PubMed

Extracytoplasmic (ECF) sigma factors, the largest class of alternative sigma factors, are related to primary sigma factors, but have simpler structures, comprising only two of six conserved functional modules in primary sigma factors: region 2 (sigmaR2) and region 4 (sigmaR4). Here, we report crystal structures of transcription initiation complexes containing Mycobacterium tuberculosis RNA polymerase (RNAP), M. tuberculosis ECF sigma factor sigma(L), and promoter DNA. The structures show that sigmaR2 and sigmaR4 of the ECF sigma factor occupy the same sites on RNAP as in primary sigma factors, show that the connector between sigmaR2 and sigmaR4 of the ECF sigma factor-although shorter and unrelated in sequence-follows the same path through RNAP as in primary sigma factors, and show that the ECF sigma factor uses the same strategy to bind and unwind promoter DNA as primary sigma factors. The results define protein-protein and protein-DNA interactions involved in ECF-sigma-factor-dependent transcription initiation.

Structural basis of ECF-sigma-factor-dependent transcription initiation.,Lin W, Mandal S, Degen D, Cho MS, Feng Y, Das K, Ebright RH Nat Commun. 2019 Feb 12;10(1):710. doi: 10.1038/s41467-019-08443-3. PMID:30755604^[6]

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

References

↑ Hu Y, Morichaud Z, Chen S, Leonetti JP, Brodolin K. Mycobacterium tuberculosis RbpA protein is a new type of transcriptional activator that stabilizes the sigma A-containing RNA polymerase holoenzyme. Nucleic Acids Res. 2012 Aug;40(14):6547-57. doi: 10.1093/nar/gks346. Epub 2012, May 8. PMID:22570422 doi:http://dx.doi.org/10.1093/nar/gks346
↑ Hu Y, Morichaud Z, Chen S, Leonetti JP, Brodolin K. Mycobacterium tuberculosis RbpA protein is a new type of transcriptional activator that stabilizes the sigma A-containing RNA polymerase holoenzyme. Nucleic Acids Res. 2012 Aug;40(14):6547-57. doi: 10.1093/nar/gks346. Epub 2012, May 8. PMID:22570422 doi:http://dx.doi.org/10.1093/nar/gks346
↑ Hu Y, Morichaud Z, Chen S, Leonetti JP, Brodolin K. Mycobacterium tuberculosis RbpA protein is a new type of transcriptional activator that stabilizes the sigma A-containing RNA polymerase holoenzyme. Nucleic Acids Res. 2012 Aug;40(14):6547-57. doi: 10.1093/nar/gks346. Epub 2012, May 8. PMID:22570422 doi:http://dx.doi.org/10.1093/nar/gks346
↑ Hahn MY, Raman S, Anaya M, Husson RN. The Mycobacterium tuberculosis extracytoplasmic-function sigma factor SigL regulates polyketide synthases and secreted or membrane proteins and is required for virulence. J Bacteriol. 2005 Oct;187(20):7062-71. doi: 10.1128/JB.187.20.7062-7071.2005. PMID:16199577 doi:http://dx.doi.org/10.1128/JB.187.20.7062-7071.2005
↑ Dainese E, Rodrigue S, Delogu G, Provvedi R, Laflamme L, Brzezinski R, Fadda G, Smith I, Gaudreau L, Palu G, Manganelli R. Posttranslational regulation of Mycobacterium tuberculosis extracytoplasmic-function sigma factor sigma L and roles in virulence and in global regulation of gene expression. Infect Immun. 2006 Apr;74(4):2457-61. PMID:16552079 doi:http://dx.doi.org/10.1128/IAI.74.4.2457-2461.2006
↑ Lin W, Mandal S, Degen D, Cho MS, Feng Y, Das K, Ebright RH. Structural basis of ECF-sigma-factor-dependent transcription initiation. Nat Commun. 2019 Feb 12;10(1):710. doi: 10.1038/s41467-019-08443-3. PMID:30755604 doi:http://dx.doi.org/10.1038/s41467-019-08443-3

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6dve"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6dve is ON HOLD
+==Crystal structure of Mycobacterium tuberculosis transcription initiation complex(ECF selenomethionine-labelled sigma factor L) with 6 nt spacer==
+<StructureSection load='6dve' size='340' side='right' caption='[[6dve]], [[Resolution|resolution]] 3.81&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6dve]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DVE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DVE FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpoA, Rv3457c, MTCY13E12.10c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU]), rpoB, Rv0667, MTCI376.08c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU]), rpoC, Rv0668, MTCI376.07c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU]), rpoZ, Rv1390, MTCY21B4.07 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU]), sigL, Rv0735 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6dve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dve OCA], [http://pdbe.org/6dve PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dve RCSB], [http://www.ebi.ac.uk/pdbsum/6dve PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dve ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/RPOZ_MYCTU RPOZ_MYCTU]] 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.<ref>PMID:22570422</ref>  [[http://www.uniprot.org/uniprot/RPOA_MYCTU RPOA_MYCTU]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00059]<ref>PMID:22570422</ref>  [[http://www.uniprot.org/uniprot/RPOC_MYCTU RPOC_MYCTU]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01322]<ref>PMID:22570422</ref>  [[http://www.uniprot.org/uniprot/RPOB_MYCTU RPOB_MYCTU]] 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/SIGL_MYCTU SIGL_MYCTU]] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis. Over-expression of SigL induces 19-28 genes including polyketide synthases, secreted and membrane proteins. Might play a minor role in regulating SigB.<ref>PMID:16199577</ref> <ref>PMID:16552079</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Extracytoplasmic (ECF) sigma factors, the largest class of alternative sigma factors, are related to primary sigma factors, but have simpler structures, comprising only two of six conserved functional modules in primary sigma factors: region 2 (sigmaR2) and region 4 (sigmaR4). Here, we report crystal structures of transcription initiation complexes containing Mycobacterium tuberculosis RNA polymerase (RNAP), M. tuberculosis ECF sigma factor sigma(L), and promoter DNA. The structures show that sigmaR2 and sigmaR4 of the ECF sigma factor occupy the same sites on RNAP as in primary sigma factors, show that the connector between sigmaR2 and sigmaR4 of the ECF sigma factor-although shorter and unrelated in sequence-follows the same path through RNAP as in primary sigma factors, and show that the ECF sigma factor uses the same strategy to bind and unwind promoter DNA as primary sigma factors. The results define protein-protein and protein-DNA interactions involved in ECF-sigma-factor-dependent transcription initiation.
-Authors: Lin, W., Das, K., Feng, Y., Ebright, R.H.
+Structural basis of ECF-sigma-factor-dependent transcription initiation.,Lin W, Mandal S, Degen D, Cho MS, Feng Y, Das K, Ebright RH Nat Commun. 2019 Feb 12;10(1):710. doi: 10.1038/s41467-019-08443-3. PMID:30755604<ref>PMID:30755604</ref>
-Description: Crystal structure of Mycobacterium tuberculosis transcription initiation complex(ECF selenomethionine-labelled sigma factor L) with 6 nt spacer
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Lin, W]]
+<div class="pdbe-citations 6dve" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: DNA-directed RNA polymerase]]
+[[Category: Myctu]]
 [[Category: Das, K]]
-[[Category: Ebright, R.H]]
+[[Category: Ebright, R H]]
 [[Category: Feng, Y]]
+[[Category: Lin, W]]
+[[Category: Ecf sigma factor]]
+[[Category: Mycobacterium tuberculosis]]
+[[Category: Rna polymerase]]
+[[Category: Transferase]]
+[[Category: Transferase-dna complex]]

6dve

From Proteopedia

Current revision

Crystal structure of Mycobacterium tuberculosis transcription initiation complex(ECF selenomethionine-labelled sigma factor L) with 6 nt spacer

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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