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-Structure paper
タイトル | The Core and Holoenzyme Forms of RNA Polymerase from . |
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ジャーナル・号・ページ | J Bacteriol, Vol. 201, Issue 4, Year 2019 |
掲載日 | 2019年2月15日 |
著者 | Tomáš Kouba / Jiří Pospíšil / Jarmila Hnilicová / Hana Šanderová / Ivan Barvík / Libor Krásný / |
PubMed 要旨 | Bacterial RNA polymerase (RNAP) is essential for gene expression and as such is a valid drug target. Hence, it is imperative to know its structure and dynamics. Here, we present two as-yet-unreported ...Bacterial RNA polymerase (RNAP) is essential for gene expression and as such is a valid drug target. Hence, it is imperative to know its structure and dynamics. Here, we present two as-yet-unreported forms of RNAP: core and holoenzyme containing σ but no other factors. Each form was detected by cryo-electron microscopy in two major conformations. Comparisons of these structures with known structures of other RNAPs reveal a high degree of conformational flexibility of the mycobacterial enzyme and confirm that region 1.1 of σ is directed into the primary channel of RNAP. Taken together, we describe the conformational changes of unrestrained mycobacterial RNAP. We describe here three-dimensional structures of core and holoenzyme forms of mycobacterial RNA polymerase (RNAP) solved by cryo-electron microscopy. These structures fill the thus-far-empty spots in the gallery of the pivotal forms of mycobacterial RNAP and illuminate the extent of conformational dynamics of this enzyme. The presented findings may facilitate future designs of antimycobacterial drugs targeting RNAP. |
リンク | J Bacteriol / PubMed:30478083 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.81 - 4.22 Å |
構造データ | |
化合物 | ChemComp-ZN: ChemComp-MG: |
由来 |
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キーワード | TRANSCRIPTION / TRANSCRIPTION Sigma |