1hk9
From Proteopedia
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CRYSTAL STRUCTURE OF THE HFQ PROTEIN FROM ESCHERICHIA COLI
Overview
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.
About this Structure
1HK9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli., Sauter C, Basquin J, Suck D, Nucleic Acids Res. 2003 Jul 15;31(14):4091-8. PMID:12853626
Page seeded by OCA on Tue Nov 20 16:37:14 2007
