1kq1
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1kq1 |SIZE=350|CAPTION= <scene name='initialview01'>1kq1</scene>, resolution 1.55Å | |PDB= 1kq1 |SIZE=350|CAPTION= <scene name='initialview01'>1kq1</scene>, resolution 1.55Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | + | |LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1kq2|1KQ2]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kq1 OCA], [http://www.ebi.ac.uk/pdbsum/1kq1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kq1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Schumacher, M A.]] | [[Category: Schumacher, M A.]] | ||
[[Category: Valentin-Hansen, P.]] | [[Category: Valentin-Hansen, P.]] | ||
| - | [[Category: ACY]] | ||
[[Category: hexamer]] | [[Category: hexamer]] | ||
[[Category: hfq]] | [[Category: hfq]] | ||
| Line 34: | Line 36: | ||
[[Category: translational regulator]] | [[Category: translational regulator]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:52:01 2008'' |
Revision as of 18:52, 30 March 2008
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| , resolution 1.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1KQ2
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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