Genome maintenance is an essential process in all cells. In prokaryotes, the RadD protein is important for survival under conditions that include DNA-damaging radiation. Precisely how RadD participates in genome maintenance remains unclear. Here we present a high-resolution X-ray crystal structure of ADP-bound Escherichia coli RadD, revealing a zinc-ribbon element that was not modelled in a previous RadD crystal structure. Insights into the mode of nucleotide binding and additional structure refinement afforded by the new RadD model will help to drive investigations into the activity of RadD as a genome stability and repair factor.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9049331PMC
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0266031PLOS

Publication Analysis

Top Keywords

crystal structure
12
x-ray crystal
8
escherichia coli
8
coli radd
8
genome maintenance
8
radd
7
structure
4
structure escherichia
4
radd dna
4
dna repair
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!