7x75: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Cryo-EM structure of Streptomyces coelicolor RNAP-promoter open complex with three Zur dimers== | ==Cryo-EM structure of Streptomyces coelicolor RNAP-promoter open complex with three Zur dimers== | ||
<StructureSection load='7x75' size='340' side='right'caption='[[7x75]]' scene=''> | <StructureSection load='7x75' size='340' side='right'caption='[[7x75]], [[Resolution|resolution]] 3.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7X75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7X75 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7x75]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7X75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7X75 FirstGlance]. <br> | ||
</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=7x75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7x75 OCA], [https://pdbe.org/7x75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7x75 RCSB], [https://www.ebi.ac.uk/pdbsum/7x75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7x75 ProSAT]</span></td></tr> | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7x75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7x75 OCA], [https://pdbe.org/7x75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7x75 RCSB], [https://www.ebi.ac.uk/pdbsum/7x75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7x75 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/A0A6G2M9E1_9ACTN A0A6G2M9E1_9ACTN]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00059] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Streptomyces coelicolor (Sc) is a model organism of actinobacteria to study morphological differentiation and production of bioactive metabolites. Sc zinc uptake regulator (Zur) affects both processes by controlling zinc homeostasis. It activates transcription by binding to palindromic Zur-box sequences upstream of -35 elements. Here we deciphered the molecular mechanism by which ScZur interacts with promoter DNA and Sc RNA polymerase (RNAP) by cryo-EM structures and biochemical assays. The ScZur-DNA structures reveal a sequential and cooperative binding of three ScZur dimers surrounding a Zur-box spaced 8 nt upstream from a -35 element. The ScRNAPsigmaHrdB-Zur-DNA structures define protein-protein and protein-DNA interactions involved in the principal housekeeping sigmaHrdB-dependent transcription initiation from a noncanonical promoter with a -10 element lacking the critical adenine residue at position -11 and a TTGCCC -35 element deviating from the canonical TTGACA motif. ScZur interacts with the C-terminal domain of ScRNAP alpha subunit (alphaCTD) in a complex structure trapped in an active conformation. Key ScZur-alphaCTD interfacial residues accounting for ScZur-dependent transcription activation were confirmed by mutational studies. Together, our structural and biochemical results provide a comprehensive model for transcription activation of Zur family regulators. | |||
Structural basis of Streptomyces transcription activation by zinc uptake regulator.,Yang X, Wang Y, Liu G, Deng Z, Lin S, Zheng J Nucleic Acids Res. 2022 Aug 12;50(14):8363-8376. doi: 10.1093/nar/gkac627. PMID:35871291<ref>PMID:35871291</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7x75" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 06:23, 8 September 2022
Cryo-EM structure of Streptomyces coelicolor RNAP-promoter open complex with three Zur dimersCryo-EM structure of Streptomyces coelicolor RNAP-promoter open complex with three Zur dimers
Structural highlights
Function[A0A6G2M9E1_9ACTN] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00059] Publication Abstract from PubMedStreptomyces coelicolor (Sc) is a model organism of actinobacteria to study morphological differentiation and production of bioactive metabolites. Sc zinc uptake regulator (Zur) affects both processes by controlling zinc homeostasis. It activates transcription by binding to palindromic Zur-box sequences upstream of -35 elements. Here we deciphered the molecular mechanism by which ScZur interacts with promoter DNA and Sc RNA polymerase (RNAP) by cryo-EM structures and biochemical assays. The ScZur-DNA structures reveal a sequential and cooperative binding of three ScZur dimers surrounding a Zur-box spaced 8 nt upstream from a -35 element. The ScRNAPsigmaHrdB-Zur-DNA structures define protein-protein and protein-DNA interactions involved in the principal housekeeping sigmaHrdB-dependent transcription initiation from a noncanonical promoter with a -10 element lacking the critical adenine residue at position -11 and a TTGCCC -35 element deviating from the canonical TTGACA motif. ScZur interacts with the C-terminal domain of ScRNAP alpha subunit (alphaCTD) in a complex structure trapped in an active conformation. Key ScZur-alphaCTD interfacial residues accounting for ScZur-dependent transcription activation were confirmed by mutational studies. Together, our structural and biochemical results provide a comprehensive model for transcription activation of Zur family regulators. Structural basis of Streptomyces transcription activation by zinc uptake regulator.,Yang X, Wang Y, Liu G, Deng Z, Lin S, Zheng J Nucleic Acids Res. 2022 Aug 12;50(14):8363-8376. doi: 10.1093/nar/gkac627. PMID:35871291[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||