The crystal structure of Rv2991 from Mycobacterium tuberculosis: An F420 binding protein with unknown function.

Affiliation

Bioorganic Chemistry and Bio-Crystallography Laboratory (B(2)Cl), Faculty of Science and Technology, Free University of Bolzano, Piazza Università 5, Bolzano 39100, Italy. Electronic address: [Email]

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.

Keywords

F(420),FDOR,Mycobacterium tuberculosis,Structural genomics,Unknown function,

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