Preliminary crystallographic analysis of recombinant VapBC‐15 toxin–antitoxin complex from Mycobacterium tuberculosis. Issue 11 (1st November 2013)

• Record Type: Journal Article
• Authors: Das, Uddipan; Kumar, Nitesh; Gourinath, Samudrala; Srinivasan, Alagiri
• Is Part Of: Acta crystallographica. Volume 69:Issue 11(2013:Nov.)
• Page Start: 1242
• Page End: 1245
• Publication Date: 2013-11-01
• Subjects: VapBC‐15 -- toxin–antitoxin -- ribonucleases -- Mycobacterium tuberculosis; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113024822
• Languages: English
• ISSNs: 1744-3091

Abstract

Abstract : The Mycobacterium tuberculosis vapBC15 locus encodes a toxin–antitoxin complex. VapC‐15 is a toxin and possesses ribonuclease activity and VapB‐15 is an antitoxin which both binds and inhibits the VapC‐15 toxin. In this study, vapBC15 genes were cloned and co‐expressed in Escherichia coli . The complex was purified to homogeneity by affinity and size‐exclusion chromatography. The VapBC‐15 complex was crystallized using the sitting‐drop vapour‐diffusion technique. The crystals diffracted to 2.6 Å resolution and belonged to space group P 21 21 21, with unit‐cell parameters a = 85.63, b = 139.09, c = 148.86 Å. The self‐rotation function combined with Matthews coefficient and solvent‐content calculations suggests the presence of either six or eight molecules of the complex in the asymmetric unit.