Crystal structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing

Yuhong Zuo, Yong Wang, Arun Malhotra

Research output: Contribution to journalArticlepeer-review

48 Scopus citations

Abstract

RNase D (RND) is one of seven exoribonucleases identified in Escherichia coli. RNase D has homologs in many eubacteria and eukaryotes, and has been shown to contribute to the 3′ maturation of several stable RNAs. Here, we report the 1.6 Å resolution crystal structure of E. coli RNase D. The conserved DEDD residues of RNase D fold into an arrangement very similar to the Klenow fragment exonuclease domain. Besides the catalytic domain, RNase D also contains two structurally similar α-helical domains with no discernible sequence homology between them. These closely resemble the HRDC domain previously seen in RecQ-family helicases and several other proteins acting on nucleic acids. More interestingly, the DEDD catalytic domain and the two helical domains come together to form a ring-shaped structure. The ring-shaped architecture of E. coli RNase D and the HRDC domains likely play a major role in determining the substrate specificity of this exoribonuclease.

Original languageEnglish (US)
Pages (from-to)973-984
Number of pages12
JournalStructure
Volume13
Issue number7
DOIs
StatePublished - Jul 2005

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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