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Updated: Jan 27, 2026

Separation and Fractionation of Culture Filtrate Proteins (CFPs) from Mycobacterium tuberculosis
Published on: July 11, 2025
The crystal structure of Rv2991 from Mycobacterium tuberculosis: An F420 binding protein with unknown function
Stefano Benini1, Ahmed Haouz2, Florence Proux2
1Bioorganic Chemistry and Bio-Crystallography Laboratory (B(2)Cl), Faculty of Science and Technology, Free University of Bolzano, Piazza Università 5, Bolzano 39100, Italy.
Abstract:
The crystal structure of the conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis has been solved by SAD using seleno-methionine substituted protein. The dimeric biological assembly and the sequence and fold conservation are typical of F420 cofactor binding enzymes. Despite Rv2991 still being of unknown function, sequence and structural comparison with similar proteins enable a role to be proposed for its C-terminal stretch of residues in recognizing and orienting the substrate. In addition, the C-terminus is involved in both protein folding and determining the size of the active site cavity.
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