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 1.55&Aring;" /> '''1.55 A Crystal struc...)
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[[Image:1kq1.gif|left|200px]]<br /><applet load="1kq1" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kq1.gif|left|200px]]<br /><applet load="1kq1" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kq1, resolution 1.55&Aring;" />
caption="1kq1, resolution 1.55&Aring;" />
'''1.55 A Crystal structure of the pleiotropic translational regulator, Hfq'''<br />
'''1.55 A Crystal structure of the pleiotropic translational regulator, Hfq'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1KQ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with ACY as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KQ1 OCA].
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1KQ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQ1 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Brennan, R.G.]]
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[[Category: Brennan, R G.]]
[[Category: Moller, T.]]
[[Category: Moller, T.]]
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[[Category: Pearson, R.F.]]
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[[Category: Pearson, R F.]]
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[[Category: Schumacher, M.A.]]
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[[Category: Schumacher, M A.]]
[[Category: Valentin-Hansen, P.]]
[[Category: Valentin-Hansen, P.]]
[[Category: ACY]]
[[Category: ACY]]
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[[Category: translational regulator]]
[[Category: translational regulator]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:45:02 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:45 2008''

Revision as of 11:36, 21 February 2008


1kq1, resolution 1.55Å

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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 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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