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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Publication : Journal of structural biology

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

Team: Crystallography
Team: Structural Microbiology
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of structural biology - 16 Mar 2019

Benini S, Haouz A, Proux F, Alzari P, Wilson K

Link to Pubmed [PMID] – 30890426

J. Struct. Biol. 2019 May;206(2):216-224

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 F 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.