PDBsum entry 4wpy

De novo protein

PDB id: 4wpy

Contents

Protein chain

88 a.a.

Ligands

TFA

GOL

Waters ×84

PDB id:

4wpy

Name:

De novo protein

Title:

Racemic crystal structure of rv1738 from mycobacterium tuberculosis (form-ii)

Structure:

Protein dl-rv1738. Chain: a. Engineered: yes

Source:

Synthetic: yes. Mycobacterium tuberculosis h37rv. Organism_taxid: 83332

Resolution:

1.50Å R-factor: 0.230 R-free: 0.253

Authors:

R.D.Bunker,K.Mandal,S.B.H.Kent,E.N.Baker

Key ref:

R.D.Bunker et al. (2015). A functional role of Rv1738 in Mycobacterium tuberculosis persistence suggested by racemic protein crystallography. Proc Natl Acad Sci U S A, 112, 4310-4315. PubMed id: 25831534 DOI: 10.1073/pnas.1422387112

Date:

21-Oct-14 Release date: 18-Mar-15

Protein chain

P9WLS2  (Y1738_MYCTO) -  Uncharacterized protein MT1780 from Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)

Seq: 94 a.a.

Struc: 88 a.a.

DOI no: 10.1073/pnas.1422387112

Proc Natl Acad Sci U S A 112:4310-4315 (2015)

PubMed id: 25831534

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

R.D.Bunker, K.Mandal, G.Bashiri, J.J.Chaston, B.L.Pentelute, J.S.Lott, S.B.Kent, E.N.Baker.

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.