4WPY: Racemic crystal structure of Rv1738 from Mycobacterium tuberculosis (Form-II)

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 translation. This suggests that the functional role of Rv1738 is to contribute to the shutdown of ribosomal protein synthesis during the onset of nonreplicating persistence of M. tuberculosis.
PDB ID: 4WPYDownload
MMDB ID: 156780
PDB Deposition Date: 2014/10/21
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 1.5  Å
Similar Structures:
Biological Unit for 4WPY: dimeric; determined by author
Molecular Components in 4WPY
Label Count Molecule
Proteins (2 molecules)
Protein Dl-rv1738
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB