Expression, purification and crystallization of phosphoribosyl transferase from a mycobacteriophage. Issue 3 (2nd March 2018)

• Record Type: Journal Article
• Authors: Li, Lei; Lee, Eungyu; Shaw, Neil
• Is Part Of: Acta crystallographica. Volume 74:Issue 3(2018:Mar.)
• Page Start: 161
• Page End: 165
• Publication Date: 2018-03-02
• Subjects: mycobacteriophages -- tuberculosis -- X‐ray diffraction -- phosphoribosyl transferases -- phage BTCU‐1; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X18002480
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : A putative phosphoribosyl transferase from phage BTCU‐1 that infects Mycobacterium and shows no sequence similarity to any structure deposited in the Protein Data Bank was cloned, expressed, purified and crystallized. The crystals diffracted X‐rays to 2.2 Å resolution. Abstract : Tuberculosis (TB) continues to remain a leading cause of death globally. Of particular concern is the emergence and rise in incidence of multidrug‐resistant and extremely drug‐resistant cases of TB. To counter this threat, it is important to explore alternative therapies, including phage therapy. Phage BTCU‐1 specifically infects Mycobacterium spp. and kills the majority of them. Intriguingly, many proteins from the phage do not share high amino‐acid sequence identity with proteins from species other than phages. Here, the expression, purification and crystallization of one such protein, a putative phosphoribosyl transferase from phage BTCU‐1, is reported. The crystals belonged to space group C 2221, with unit‐cell parameters a = 59.71, b = 64.42, c = 65.32 Å, α = β = γ = 90°. The crystals diffracted X‐rays to 2.2 Å resolution.