6heg

Publication Abstract from PubMed

RNA helicases are almost ubiquitous important enzymes that take part in multiple aspects of RNA metabolism. Prokaryotes encode fewer RNA helicases than eukaryotes, suggesting that individual prokaryotic RNA helicases may take on multiple roles. The specific functions and molecular mechanisms of bacterial DEAH/RHA helicases are poorly understood, and no structures are available of these bacterial enzymes. Here, we report the first crystal structure of the DEAH/RHA helicase HrpB of Escherichia coli in a complex with ADP*AlF4. It showed an atypical globular structure, consisting of two RecA domains, an HA2 domain and an OB domain, similar to eukaryotic DEAH/RHA helicases. Notably, it showed a unique C-terminal extension that has never been reported before. Activity assays indicated that EcHrpB binds RNA but not DNA, and does not exhibit unwinding activity in vitro. Thus, within cells, the EcHrpB may function in helicase activity-independent RNA metabolic processes.

Crystal structure of Escherichia coli DEAH/RHA helicase HrpB.,Xin BG, Chen WF, Rety S, Dai YX, Xi XG Biochem Biophys Res Commun. 2018 Sep 26;504(1):334-339. doi:, 10.1016/j.bbrc.2018.08.191. Epub 2018 Sep 4. PMID:30190128^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.