6F6W

Structure of Mycobacterium smegmatis RNA polymerase core

Summary for 6F6W

• Entry DOI: 10.2210/pdb6f6w/pdb
• Related: 6EYD
• EMDB information: 3983 4192
• Descriptor: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (6 entities in total)
• Functional Keywords: transcription sigma, transcription
• Biological source: Mycolicibacterium smegmatis MC2 155; More
• Total number of polymer chains: 5
• Total formula weight: 364829.59

Authors

Kouba, T.,Barvik, I.,Krasny, L. (deposition date: 2017-12-06, release date: 2018-12-19, Last modification date: 2024-05-15)

Primary citation

Kouba, T.,Pospisil, J.,Hnilicova, J.,Sanderova, H.,Barvik, I.,Krasny, L.
The Core and Holoenzyme Forms of RNA Polymerase fromMycobacterium smegmatis.
J. Bacteriol., 201:-, 2019

PubMed Abstract: 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.

PubMed: 30478083
DOI: 10.1128/JB.00583-18

Experimental method

ELECTRON MICROSCOPY (3.81 Å)