1kq2: Difference between revisions

Revision as of 14:36, 21 February 2008

Crystal Structure of an Hfq-RNA Complex

OverviewOverview

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 StructureAbout this Structure

1KQ2 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

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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OCA

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-[[Image:1kq2.gif|left|200px]]<br /><applet load="1kq2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1kq2.gif|left|200px]]<br /><applet load="1kq2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1kq2, resolution 2.71&Aring;" />
 '''Crystal Structure of an Hfq-RNA Complex'''<br />
 ==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.
+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==
-KQ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KQ2 OCA].
+KQ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQ2 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Staphylococcus aureus]]
-[[Category: Brennan, R.G.]]
+[[Category: Brennan, R G.]]
 [[Category: Moller, T.]]
-[[Category: Pearson, R.F.]]
+[[Category: Pearson, R F.]]
-[[Category: Schumacher, M.A.]]
+[[Category: Schumacher, M A.]]
 [[Category: Valentin-Hansen, P.]]
 [[Category: hfq-rna complex]]
@@ Line 22: / Line 22: @@
 [[Category: translational regulator]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:45:25 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:45 2008''