6HEG
Crystal structure of Escherichia coli DEAH/RHA helicase HrpB
Summary for 6HEG
| Entry DOI | 10.2210/pdb6heg/pdb |
| Descriptor | ATP-dependent RNA helicase HrpB, ADENOSINE-5'-DIPHOSPHATE, TETRAFLUOROALUMINATE ION, ... (4 entities in total) |
| Functional Keywords | deah/rha helicase rna helicase, hydrolase |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 1 |
| Total formula weight | 90347.69 |
| Authors | Xin, B.G.,Chen, W.F.,Rety, S.,Dai, Y.X.,Xi, X.G. (deposition date: 2018-08-20, release date: 2018-09-12, Last modification date: 2024-01-17) |
| Primary citation | Xin, B.G.,Chen, W.F.,Rety, S.,Dai, Y.X.,Xi, X.G. Crystal structure of Escherichia coli DEAH/RHA helicase HrpB. Biochem. Biophys. Res. Commun., 504:334-339, 2018 Cited by PubMed Abstract: 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•AlF. 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. PubMed: 30190128DOI: 10.1016/j.bbrc.2018.08.191 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.019 Å) |
Structure validation
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