Structure of bacterial LigD 3′-phosphoesterase unveils a DNA repair superfamily Journal Article
| Authors: | Nair, P. A.; Smith, P.; Shuman, S. |
| Article Title: | Structure of bacterial LigD 3′-phosphoesterase unveils a DNA repair superfamily |
| Abstract: | The DNA ligase D (LigD) 3′-phosphoesterase (PE) module is a conserved component of the bacterial nonhomologous end-joining (NHEJ) apparatus that performs 3′ end-healing reactions at DNA double-strand breaks. Here we report the 1.9 Å crystal structure of Pseudomonas aeruginosa PE, which reveals that PE exemplifies a unique class of DNA repair enzyme. PE has a distinctive fold in which an eight stranded β barrel with a hydrophobic interior supports a crescent-shaped hydrophilic active site on its outer surface. Six essential side chains coordinate manganese and a sulfate mimetic of the scissile phosphate. The PE active site and mechanism are unique vis à vis other end-healing enzymes. We find PE homologs in archaeal and eukaryal proteomes, signifying that PEs comprise a DNA repair superfamily. |
| Keywords: | unclassified drug; nonhuman; proteome; dna repair; phosphatase; bacteria (microorganisms); double stranded dna; amino acid sequence; molecular sequence data; eukaryota; dna repair enzymes; crystal structure; crystallography, x-ray; protein structure, tertiary; catalysis; crystallization; polydeoxyribonucleotide synthase; catalytic domain; archaea; eukaryote; biocatalysis; multigene family; esterases; dna ligases; bacterial gene; hydrophilicity; pseudomonas aeruginosa; bacterial cell; 3′ end-healing; nonhomologous end-joining; 3' phosphoesterase; archaeal protein; dna homolog; dna ligase d; manganese |
| Journal Title: | Proceedings of the National Academy of Sciences of the United States of America |
| Volume: | 107 |
| Issue: | 29 |
| ISSN: | 0027-8424 |
| Publisher: | National Academy of Sciences |
| Date Published: | 2010-07-20 |
| Start Page: | 12822 |
| End Page: | 12827 |
| Language: | English |
| DOI: | 10.1073/pnas.1005830107 |
| PUBMED: | 20616014 |
| PROVIDER: | scopus |
| PMCID: | PMC2919965 |
| DOI/URL: | |
| Notes: | --- - "Export Date: 20 April 2011" - "CODEN: PNASA" - "Source: Scopus" |
Altmetric
Citation Impact
BMJ Impact Analytics
Related MSK Work