%0 Journal Article %T The crystal structure of Rv2991 from Mycobacterium tuberculosis: An F420 binding protein with unknown function %+ Free University of Bozen-Bolzano %+ Cristallographie (Plateforme) - Crystallography (Platform) %+ Microbiologie structurale - Structural Microbiology (Microb. Struc. (UMR_3528 / U-Pasteur_5)) %+ Department of Chemistry [York University - Toronto] %A Benini, Stefano %A Haouz, Ahmed %A Proux, Florence %A Alzari, Pedro %A Wilson, Keith %Z The work was supported by a grant from the 5th PCRDT program of the European Union (acronym X-TB). The authors thank the EU for support through the grant ‘Structural and Functional Genomics of Mycobacterium tuberculosis’ (QLK2-CT-2001-02018). We thank the staff of the recombinant protein platform at the Institut Pasteur for the production and purification of Rv2991. %< avec comité de lecture %@ 1047-8477 %J Journal of Structural Biology %I Elsevier %V 206 %N 2 %P 216-224 %8 2019-05 %D 2019 %R 10.1016/j.jsb.2019.03.006 %M 30890426 %K F(420) %K FDOR %K Mycobacterium tuberculosis %K Structural genomics %K Unknown function %Z Chemical Sciences/Cristallography %Z Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] %Z Life Sciences [q-bio]/Biochemistry, Molecular Biology %Z Computer Science [cs]/Bioinformatics [q-bio.QM] %Z Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph] %Z Life Sciences [q-bio]/Cellular BiologyJournal articles %X 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. %G English %L pasteur-03095980 %U https://pasteur.hal.science/pasteur-03095980 %~ PASTEUR %~ CNRS