4yg2
From Proteopedia
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| - | ''' | + | ==X-ray crystal structur of Escherichia coli RNA polymerase sigma70 holoenzyme== |
| + | <StructureSection load='4yg2' size='340' side='right' caption='[[4yg2]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4yg2]] is a 12 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yfk|4yfk]], [[4yfn|4yfn]], [[4yfx|4yfx]], [[4igc|4igc]]</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=4yg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yg2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yg2 RCSB], [http://www.ebi.ac.uk/pdbsum/4yg2 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/RPOZ_ECO57 RPOZ_ECO57]] 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 (By similarity). [[http://www.uniprot.org/uniprot/RPOA_ECO57 RPOA_ECO57]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[http://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. [[http://www.uniprot.org/uniprot/RPOB_ECO57 RPOB_ECO57]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[http://www.uniprot.org/uniprot/RPOD_ECOLI RPOD_ECOLI]] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This is the primary sigma factor of this bacterium. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Escherichia 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<ref>PMID:23389035</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Murakami, K | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: DNA-directed RNA polymerase]] | ||
| + | [[Category: Murakami, K S]] | ||
| + | [[Category: Rna polymerase]] | ||
| + | [[Category: Transferase-transcription complex]] | ||
Revision as of 11:57, 18 March 2015
X-ray crystal structur of Escherichia coli RNA polymerase sigma70 holoenzyme
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