Structural highlights
6jde is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | |
| Gene: | radD, yejH, yejI, yejJ, b2184, JW2172 (ECOLI) |
| Activity: | DNA helicase, with EC number 3.6.4.12 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[RADD_ECOLI] May be a helicase. In combination with RadA is important in repair of double-strand DNA breaks (DSB) (PubMed:25425430, PubMed:25484163).[1] [2]
Publication Abstract from PubMed
The helicase superfamily 2 (SF2) proteins are involved in essentially every step in DNA and RNA metabolism. The radD (yejH) gene, which belongs to SF2, plays an important role in DNA repair. The RadD protein includes all seven conserved SF2 motifs and has shown ATPase activity. Here, we first reported the structure of RadD from Escherichia coli containing two RecA-like domains, a zinc finger motif, and a C-terminal domain. Based on the structure of RadD and other SF2 proteins, we then built a model of the RedD-ATP complex.
Crystal structure of a novel ATPase RadD from Escherichia coli.,Kuang X, Tang Q, Liu YP, Yan XX, Xu W Proteins. 2019 Apr 29. doi: 10.1002/prot.25704. PMID:31035307[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen SH, Byrne RT, Wood EA, Cox MM. Escherichia coli radD (yejH) gene: a novel function involved in radiation resistance and double-strand break repair. Mol Microbiol. 2015 Mar;95(5):754-68. doi: 10.1111/mmi.12885. Epub 2015 Jan 16. PMID:25425430 doi:http://dx.doi.org/10.1111/mmi.12885
- ↑ Cooper DL, Boyle DC, Lovett ST. Genetic analysis of Escherichia coli RadA: functional motifs and genetic interactions. Mol Microbiol. 2015 Mar;95(5):769-79. doi: 10.1111/mmi.12899. Epub 2015 Jan 30. PMID:25484163 doi:http://dx.doi.org/10.1111/mmi.12899
- ↑ Kuang X, Tang Q, Liu YP, Yan XX, Xu W. Crystal structure of a novel ATPase RadD from Escherichia coli. Proteins. 2019 Apr 29. doi: 10.1002/prot.25704. PMID:31035307 doi:http://dx.doi.org/10.1002/prot.25704
