Fig. 1: Single-particle cryo-EM structure of the M. tuberculosis Rho complex. | Communications Biology

Fig. 1: Single-particle cryo-EM structure of the M. tuberculosis Rho complex.

From: Cryo-EM structure of transcription termination factor Rho from Mycobacterium tuberculosis reveals bicyclomycin resistance mechanism

Fig. 1: Single-particle cryo-EM structure of the M. tuberculosis Rho complex.The alternative text for this image may have been generated using AI.

a–c The 3.3 Å cryo-map of MtbRho colored according to local resolution from highest (dark blue) to lowest resolution (dark purple). The MtbRho is composed of six subunits adopting an open corkscrew conformation. When observed from top (a) or down (b) views, MtbRho displays a U-like shape where the two subunits at the gap are the less well-resolved (black dots) while the innermost subunits (black stars) are the best resolved. The side view c highlights the shift between the two gap subunits that results from the corkscrew arrangement of the MtbRho ring. The first ~220 N-terminal residues of each protomer are not resolved. d Close-up view of the ATP binding site at the C/D interface. The MtbRho atomic model and cryo-EM map are superimposed. The ATP phosphates are in orange, sugar in green, oxygen groups in red and adenine base in green/blue. The catalytic Mg2+ ion is shown as a green sphere. e Refined PDB structure of MtbRho. The subunits are labeled from A to F in clockwise order, observed from the CTD face of the MtbRho hexamer as in B.

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