A functional role of Rv1738 in Mycobacterium tuberculosis persistence suggested by racemic protein crystallography.

ABSTRACT: Protein 3D structure can be a powerful predictor of function, but it often faces a critical roadblock at the crystallization step. Rv1738, a protein from Mycobacterium tuberculosis that is strongly implicated in the onset of nonreplicating persistence, and thereby latent tuberculosis, resisted extensive attempts at crystallization. Chemical synthesis of the L- and D-enantiomeric forms of Rv1738 enabled facile crystallization of the D/L-racemic mixture. The structure was solved by an ab initio approach that took advantage of the quantized phases characteristic of diffraction by centrosymmetric crystals. The structure, containing L- and D-dimers in a centrosymmetric space group, revealed unexpected homology with bacterial hibernation-promoting factors that bind to ribosomes and suppress tran

SUBMITTER: Bunker RD 

PROVIDER: S-EPMC4394262 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature