8hkc: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8hkc]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [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=8HKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HKC FirstGlance]. <br> | <table><tr><td colspan='2'>[[8hkc]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [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=8HKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HKC FirstGlance]. <br> | ||
</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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.49Å</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=8hkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hkc OCA], [https://pdbe.org/8hkc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hkc RCSB], [https://www.ebi.ac.uk/pdbsum/8hkc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hkc ProSAT]</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=8hkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hkc OCA], [https://pdbe.org/8hkc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hkc RCSB], [https://www.ebi.ac.uk/pdbsum/8hkc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hkc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://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] | [https://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] | ||
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== Publication Abstract from PubMed == | |||
Bacterial RNA polymerases (RNAP) form distinct holoenzymes with different sigma factors to initiate diverse gene expression programs. In this study, we report a cryo-EM structure at 2.49 A of RNA polymerase transcription complex containing a temperature-sensitive bacterial sigma factor, sigma(32) (sigma(32)-RPo). The structure of sigma(32)-RPo reveals key interactions essential for the assembly of E. coli sigma(32)-RNAP holoenzyme and for promoter recognition and unwinding by sigma(32). Specifically, a weak interaction between sigma(32) and -35/-10 spacer is mediated by T128 and K130 in sigma(32). A histidine in sigma(32), rather than a tryptophan in sigma(70), acts as a wedge to separate the base pair at the upstream junction of the transcription bubble, highlighting the differential promoter-melting capability of different residue combinations. Structure superimposition revealed relatively different orientations between betaFTH and sigma(4) from other sigma-engaged RNAPs and biochemical data suggest that a biased sigma(4)-betaFTH configuration may be adopted to modulate binding affinity to promoter so as to orchestrate the recognition and regulation of different promoters. Collectively, these unique structural features advance our understanding of the mechanism of transcription initiation mediated by different sigma factors. | |||
Structural Insight into the Mechanism of sigma32-Mediated Transcription Initiation of Bacterial RNA Polymerase.,Lu Q, Chen T, Wang J, Wang F, Ye W, Ma L, Wu S Biomolecules. 2023 Apr 25;13(5):738. doi: 10.3390/biom13050738. PMID:37238608<ref>PMID:37238608</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 8hkc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||