1HK9
Crystal structure of the Hfq protein from Escherichia coli
Summary for 1HK9
| Entry DOI | 10.2210/pdb1hk9/pdb |
| Descriptor | PROTEIN HFQ (2 entities in total) |
| Functional Keywords | rna-binding protein, sm-like, pleiotropic regulator, rna binding protein, rna chaperone |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 6 |
| Total formula weight | 49545.43 |
| Authors | Sauter, C.,Basquin, J.,Suck, D. (deposition date: 2003-03-06, release date: 2003-07-24, Last modification date: 2023-12-13) |
| Primary citation | Sauter, C.,Basquin, J.,Suck, D. Sm-Like Proteins in Eubacteria: The Crystal Structure of the Hfq Protein from Escherichia Coli Nucleic Acids Res., 31:4091-, 2003 Cited by PubMed Abstract: The Hfq protein was discovered in Escherichia coli in the early seventies as a host factor for the Qbeta phage RNA replication. During the last decade, it was shown to be involved in many RNA processing events and remote sequence homology indicated a link to spliceosomal Sm proteins. We report the crystal structure of the E.coli Hfq protein showing that its monomer displays a characteristic Sm-fold and forms a homo-hexamer, in agreement with former biochemical data. Overall, the structure of the E.coli Hfq ring is similar to the one recently described for Staphylococcus aureus. This confirms that bacteria contain a hexameric Sm-like protein which is likely to be an ancient and less specialized form characterized by a relaxed RNA binding specificity. In addition, we identified an Hfq ortholog in the archaeon Methanococcus jannaschii which lacks a classical Sm/Lsm gene. Finally, a detailed structural comparison shows that the Sm-fold is remarkably well conserved in bacteria, Archaea and Eukarya, and represents a universal and modular building unit for oligomeric RNA binding proteins. PubMed: 12853626DOI: 10.1093/NAR/GKG480 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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