3lu0
From Proteopedia
(Difference between revisions)
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<SX load='3lu0' size='340' side='right' viewer='molstar' caption='[[3lu0]], [[Resolution|resolution]] 11.20Å' scene=''> | <SX load='3lu0' size='340' side='right' viewer='molstar' caption='[[3lu0]], [[Resolution|resolution]] 11.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3lu0]] is a 5 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3lu0]] is a 5 chain structure with sequence from [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=3LU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LU0 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 11.2Å</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=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lu0 OCA], [https://pdbe.org/3lu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lu0 RCSB], [https://www.ebi.ac.uk/pdbsum/3lu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lu0 ProSAT]</span></td></tr> |
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- | <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/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] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lu0 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lu0 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The Escherichia coli transcription system is the best characterized from a biochemical and genetic point of view and has served as a model system. Nevertheless, a molecular understanding of the details of E. coli transcription and its regulation, and therefore its full exploitation as a model system, has been hampered by the absence of high-resolution structural information on E. coli RNA polymerase (RNAP). We use a combination of approaches, including high-resolution X-ray crystallography, ab initio structural prediction, homology modeling, and single-particle cryo-electron microscopy, to generate complete atomic models of E. coli core RNAP and an E. coli RNAP ternary elongation complex. The detailed and comprehensive structural descriptions can be used to help interpret previous biochemical and genetic data in a new light and provide a structural framework for designing experiments to understand the function of the E. coli lineage-specific insertions and their role in the E. coli transcription program. | ||
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- | Complete structural model of Escherichia coli RNA polymerase from a hybrid approach.,Opalka N, Brown J, Lane WJ, Twist KA, Landick R, Asturias FJ, Darst SA PLoS Biol. 2010 Sep 14;8(9). pii: e1000483. PMID:20856905<ref>PMID:20856905</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 3lu0" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
- | [[Category: | + | [[Category: Escherichia coli K-12]] |
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Darst | + | [[Category: Darst SA]] |
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Current revision
Molecular model of Escherichia coli core RNA polymerase
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