4yg2: Difference between revisions
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<StructureSection load='4yg2' size='340' side='right'caption='[[4yg2]], [[Resolution|resolution]] 3.70Å' scene=''> | <StructureSection load='4yg2' size='340' side='right'caption='[[4yg2]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4yg2]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4yg2]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4igc 4igc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YG2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | </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=4yg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yg2 OCA], [https://pdbe.org/4yg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yg2 RCSB], [https://www.ebi.ac.uk/pdbsum/4yg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yg2 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/RPOC_ECO57 RPOC_ECO57] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 23: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[RNA polymerase|RNA polymerase]] | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
*[[Sigma factor|Sigma factor]] | *[[Sigma factor 3D structures|Sigma factor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: | [[Category: Escherichia coli O157:H7]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Murakami | [[Category: Murakami KS]] | ||
Revision as of 11:12, 3 May 2023
X-ray crystal structur of Escherichia coli RNA polymerase sigma70 holoenzymeX-ray crystal structur of Escherichia coli RNA polymerase sigma70 holoenzyme
Structural highlights
FunctionRPOC_ECO57 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Publication Abstract from PubMedEscherichia coli RNA polymerase (RNAP) is the most studied bacterial RNAP and has been used as the model RNAP for screening and evaluating potential RNAP-targeting antibiotics. However, the x-ray crystal structure of E. coli RNAP has been limited to individual domains. Here, I report the x-ray structure of the E. coli RNAP sigma(70) holoenzyme, which shows sigma region 1.1 (sigma1.1) and the alpha subunit C-terminal domain for the first time in the context of an intact RNAP. sigma1.1 is positioned at the RNAP DNA-binding channel and completely blocks DNA entry to the RNAP active site. The structure reveals that sigma1.1 contains a basic patch on its surface, which may play an important role in DNA interaction to facilitate open promoter complex formation. The alpha subunit C-terminal domain is positioned next to sigma domain 4 with a fully stretched linker between the N- and C-terminal domains. E. coli RNAP crystals can be prepared from a convenient overexpression system, allowing further structural studies of bacterial RNAP mutants, including functionally deficient and antibiotic-resistant RNAPs. X-ray crystal structure of Escherichia coli RNA polymerase sigma70 holoenzyme.,Murakami KS J Biol Chem. 2013 Mar 29;288(13):9126-34. doi: 10.1074/jbc.M112.430900. Epub 2013, Feb 6. PMID:23389035[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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