5IUF
Bacillus NanoRNase A active site mutant bound to pAp
Summary for 5IUF
| Entry DOI | 10.2210/pdb5iuf/pdb |
| Related | 5IPP |
| Descriptor | Bifunctional oligoribonuclease and PAP phosphatase NrnA, ADENOSINE-3'-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | nanorna; rna degradation; exonuclease; rnase; b. subtilis; x-ray; abortive transcripts; pap phosphatase, hydrolase |
| Biological source | Bacillus subtilis (strain 168) |
| Total number of polymer chains | 4 |
| Total formula weight | 151375.98 |
| Authors | Schmier, B.J.,Nelersa, C.M.,Malhotra, A. (deposition date: 2016-03-17, release date: 2017-08-02, Last modification date: 2023-09-27) |
| Primary citation | Schmier, B.J.,Nelersa, C.M.,Malhotra, A. Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA. Sci Rep, 7:11085-11085, 2017 Cited by PubMed Abstract: NanoRNAs are RNA fragments 2 to 5 nucleotides in length that are generated as byproducts of RNA degradation and abortive transcription initiation. Cells have specialized enzymes to degrade nanoRNAs, such as the DHH phosphoesterase family member NanoRNase A (NrnA). This enzyme was originally identified as a 3' → 5' exonuclease, but we show here that NrnA is bidirectional, degrading 2-5 nucleotide long RNA oligomers from the 3' end, and longer RNA substrates from the 5' end. The crystal structure of Bacillus subtilis NrnA reveals a dynamic bi-lobal architecture, with the catalytic N-terminal DHH domain linked to the substrate binding C-terminal DHHA1 domain via an extended linker. Whereas this arrangement is similar to the structure of RecJ, a 5' → 3' DHH family DNase and other DHH family nanoRNases, Bacillus NrnA has gained an extended substrate-binding patch that we posit is responsible for its 3' → 5' activity. PubMed: 28894100DOI: 10.1038/s41598-017-09403-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
Download full validation report
