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Publication Abstract from PubMed

MabR (Rv2242), a PucR-type transcription factor, plays a crucial role in regulating mycolic acid biosynthesis in Mycobacterium tuberculosis. To understand its regulatory mechanisms, we determined the crystal structures of its N-terminal and C-terminal domains. The N-terminal domain adopts a globin-like fold, while the C-terminal domain comprises an alpha/beta GGDEF domain and an all-alpha effector domain with a helix-turn-helix DNA-binding motif. This unique domain combination is specific to Actinomycetes. Biochemical and computational studies suggest that full-length MabR forms both dimeric and tetrameric assemblies in solution. Structural analysis revealed two distinct dimerization interfaces within the N- and C-terminal domains, further supporting a tetrameric organization. These findings provide valuable insights into the domain architecture, oligomeric state, and potential regulatory mechanisms of MabR.

Domain architecture of the Mycobacterium tuberculosis MabR (Rv2242), a member of the PucR transcription factor family.,Megalizzi V, Tanina A, Grosse C, Mirgaux M, Legrand P, Dias Mirandela G, Wohlkonig A, Bifani P, Wintjens R Heliyon. 2024 Nov 16;10(22):e40494. doi: 10.1016/j.heliyon.2024.e40494. , eCollection 2024 Nov 30. PMID:39641026^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.