View source for 8dkc


==P. gingivalis RNA Polymerase==
<StructureSection load='8dkc' size='340' side='right'caption='[[8dkc]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8dkc]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyromonas_gingivalis Porphyromonas gingivalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DKC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#8491;</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=8dkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dkc OCA], [https://pdbe.org/8dkc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dkc RCSB], [https://www.ebi.ac.uk/pdbsum/8dkc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dkc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RPOA_PORGI RPOA_PORGI] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00059]
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== Publication Abstract from PubMed ==
Porphyromonas gingivalis, an anaerobic CFB (Cytophaga, Fusobacterium, and Bacteroides) group bacterium, is the keystone pathogen of periodontitis and has been implicated in various systemic diseases. Increased antibiotic resistance and lack of effective antibiotics necessitate a search for new intervention strategies. Here we report a 3.5 A resolution cryo-EM structure of P. gingivalis RNA polymerase (RNAP). The structure displays new structural features in its omega subunit and multiple domains in beta and beta' subunits, which differ from their counterparts in other bacterial RNAPs. Superimpositions with E. coli RNAP holoenzyme and initiation complex further suggest that its omega subunit may contact the sigma4 domain, thereby possibly contributing to the assembly and stabilization of initiation complexes. In addition to revealing the unique features of P. gingivalis RNAP, our work offers a framework for future studies of transcription regulation in this important pathogen, as well as for structure-based drug development.

Cryo-EM Structure of Porphyromonas gingivalis RNA Polymerase.,Bu F, Wang X, Li M, Ma L, Wang C, Hu Y, Cao Z, Liu B J Mol Biol. 2024 May 15;436(10):168568. doi: 10.1016/j.jmb.2024.168568. Epub 2024 , Apr 5. PMID:38583515<ref>PMID:38583515</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Porphyromonas gingivalis]]
[[Category: Bu F]]
[[Category: Liu B]]