4WSP

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

4WSP の概要

• エントリーDOI: 10.2210/pdb4wsp/pdb
• 関連するPDBエントリー: 4WPY
• 分子名称: protein DL-Rv1738, CHLORIDE ION (3 entities in total)
• 機能のキーワード: hypoxic response, de novo protein
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10659.53

構造登録者

Bunker, R.D.,Mandal, K.,Kent, S.B.H.,Baker, E.N. (登録日: 2014-10-28, 公開日: 2015-03-18, 最終更新日: 2023-09-27)

主引用文献

Bunker, R.D.,Mandal, K.,Bashiri, G.,Chaston, J.J.,Pentelute, B.L.,Lott, J.S.,Kent, S.B.,Baker, E.N.
A functional role of Rv1738 in Mycobacterium tuberculosis persistence suggested by racemic protein crystallography.
Proc.Natl.Acad.Sci.USA, 112:4310-4315, 2015

PubMed 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 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.

PubMed: 25831534
DOI: 10.1073/pnas.1422387112

実験手法

X-RAY DIFFRACTION (1.65 Å)