1hk9: Difference between revisions

Revision as of 14:02, 21 February 2008

CRYSTAL STRUCTURE OF THE HFQ PROTEIN FROM ESCHERICHIA COLI

OverviewOverview

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 StructureAbout this Structure

1HK9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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

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-[[Image:1hk9.jpg|left|200px]]<br /><applet load="1hk9" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1hk9, resolution 2.15&Aring;" />
 '''CRYSTAL STRUCTURE OF THE HFQ PROTEIN FROM ESCHERICHIA COLI'''<br />
 ==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.
+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==
-HK9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HK9 OCA].
+HK9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HK9 OCA].
 ==Reference==
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 [[Category: sm-like]]
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