4wpy | pdb_00004wpy

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

spinqualitylabelsall models 4wpy, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wpy is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, TFA Related: 4wsp Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. A functional role of Rv1738 in Mycobacterium tuberculosis persistence suggested by racemic protein crystallography.,Bunker RD, Mandal K, Bashiri G, Chaston JJ, Pentelute BL, Lott JS, Kent SB, Baker EN Proc Natl Acad Sci U S A. 2015 Apr 7;112(14):4310-5. doi:, 10.1073/pnas.1422387112. Epub 2015 Mar 23. PMID:25831534 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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