1kq1
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(New page: 200px<br /><applet load="1kq1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kq1, resolution 1.55Å" /> '''1.55 A Crystal struc...)
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Revision as of 23:37, 24 November 2007
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1.55 A Crystal structure of the pleiotropic translational regulator, Hfq
Overview
In prokaryotes, Hfq regulates translation by modulating the structure of, numerous RNA molecules by binding preferentially to A/U-rich sequences. To, elucidate the mechanisms of target recognition and translation regulation, by Hfq, we determined the crystal structures of the Staphylococcus aureus, Hfq and an Hfq-RNA complex to 1.55 and 2.71 A resolution, respectively., The structures reveal that Hfq possesses the Sm-fold previously observed, only in eukaryotes and archaea. However, unlike these heptameric Sm, proteins, Hfq forms a homo-hexameric ring. The Hfq-RNA structure reveals, that the single-stranded hepta-oligoribonucleotide binds in a circular, conformation around a central basic cleft, whereby Tyr42 residues from, adjacent subunits stack with six of the bases, and Gln8, outside the Sm, motif, provides key protein-base contacts. Such binding suggests a, mechanism for Hfq function.
About this Structure
1KQ1 is a Single protein structure of sequence from Staphylococcus aureus with ACY as ligand. Full crystallographic information is available from OCA.
Reference
Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein., Schumacher MA, Pearson RF, Moller T, Valentin-Hansen P, Brennan RG, EMBO J. 2002 Jul 1;21(13):3546-56. PMID:12093755
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