5IPP

Structure of Bacillus NanoRNase A active site mutant bound to a mononucleotide

5IPP の概要

• エントリーDOI: 10.2210/pdb5ipp/pdb
• 関連するPDBエントリー: 5IUF
• 分子名称: Bifunctional oligoribonuclease and PAP phosphatase NrnA, ADENOSINE MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: nanorna, rna degradation, exonuclease, rnase, abortive transcripts, pap phosphatase, hydrolase
• 由来する生物種: Bacillus subtilis (strain 168)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 150361.61

構造登録者

Schmier, B.J.,Nelersa, C.M.,Malhotra, A. (登録日: 2016-03-09, 公開日: 2017-08-02, 最終更新日: 2024-03-06)

主引用文献

Schmier, B.J.,Nelersa, C.M.,Malhotra, A.
Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA.
Sci Rep, 7:11085-11085, 2017

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: 28894100
DOI: 10.1038/s41598-017-09403-x

実験手法

X-RAY DIFFRACTION (1.95 Å)