6iz2

Publication Abstract from PubMed

Deinococcus radiodurans is an extremophilic bacterium well-known for its extraordinary resistance to ionizing radiation and other DNA damage- and oxidative stress-generating agents. In addition to its efficient DNA damage repair and oxidative stress resistance mechanisms, protein family expansions and stress-induced genes/proteins are also regarded as important components that add to the robustness of this bacterium. D. radiodurans encodes specific expansions of 13 DinB/YfiT homologs, which is a relatively large number when compared to those found in Gram-positive bacteria. In this study, we investigated the expression profiles of 13 dinB genes after gamma-irradiation, mitomycin C and H2O2 treatment. dr0053 had the highest expression levels after DNA-damage inducing gamma-irradiation and MMC treatment, increasing approximately 200-fold and approximately 16-fold, respectively. We also determined the crystal structure of DR0053 at 2.07A resolution. DR0053 adopted a typical four-helix bundle structure that is characteristic of DinB/YfiT proteins. A putative metal binding site was occupied by zinc even though the highly conserved His triad of DinB/YfiT proteins was replaced by Glu-Asn-His.

Crystal structure of the highly radiation-inducible DinB/YfiT superfamily protein DR0053 from Deinococcus radiodurans R1.,Zhang J, Zhao L, Seo HS, Jung JH, Choi JI, Kim MK, Lim S Biochem Biophys Res Commun. 2019 May 28;513(2):354-359. doi:, 10.1016/j.bbrc.2019.03.209. Epub 2019 Apr 5. PMID:30961930^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.