1kq2: Difference between revisions
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|PDB= 1kq2 |SIZE=350|CAPTION= <scene name='initialview01'>1kq2</scene>, resolution 2.71Å | |PDB= 1kq2 |SIZE=350|CAPTION= <scene name='initialview01'>1kq2</scene>, resolution 2.71Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1kq1|1KQ1]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kq2 OCA], [http://www.ebi.ac.uk/pdbsum/1kq2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kq2 RCSB]</span> | |||
}} | }} | ||
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[[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 21:51:56 2008'' | ||
Revision as of 21:51, 30 March 2008
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| , resolution 2.71Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1KQ1
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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