This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1kq2
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1kq2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kq2, resolution 2.71Å" /> '''Crystal Structure of...)
Next diff →
Revision as of 23:37, 24 November 2007
|
Crystal Structure of an Hfq-RNA Complex
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
1KQ2 is a Single protein structure of sequence from Staphylococcus aureus. 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
Page seeded by OCA on Sun Nov 25 01:45:25 2007
