9F80

Crystal structure of Rv2242 regulator C-terminal fragment (161-414)

Summary for 9F80

• Entry DOI: 10.2210/pdb9f80/pdb
• Descriptor: Uncharacterized protein Rv2242, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, SODIUM ION, ... (4 entities in total)
• Functional Keywords: helix-turn-helix, pucr family, transcription, tuberculosis, dna binding protein
• Biological source: Mycobacterium tuberculosis H37Rv
• Total number of polymer chains: 1
• Total formula weight: 29251.97

Authors

Megalizzi, V.,Tanina, A.,Grosse, C.,Mirgaux, M.,Legrand, P.,Dias Mirandela, G.,Wohlkonig, A.,Bifani, P.,Wintjens, R. (deposition date: 2024-05-06, release date: 2024-12-18)

Primary citation

Megalizzi, V.,Tanina, A.,Grosse, C.,Mirgaux, M.,Legrand, P.,Dias Mirandela, G.,Wohlkonig, A.,Bifani, P.,Wintjens, R.
Domain architecture of the Mycobacterium tuberculosis MabR ( Rv2242 ), a member of the PucR transcription factor family.
Heliyon, 10:e40494-e40494, 2024

PubMed Abstract: MabR (), a PucR-type transcription factor, plays a crucial role in regulating mycolic acid biosynthesis in . 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 α/β GGDEF domain and an all-α effector domain with a helix-turn-helix DNA-binding motif. This unique domain combination is specific to . 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.

PubMed: 39641026
DOI: 10.1016/j.heliyon.2024.e40494

Experimental method

X-RAY DIFFRACTION (2.027 Å)