1kq2: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='1kq2' size='340' side='right'caption='[[1kq2]], [[Resolution|resolution]] 2.71Å' scene=''> | <StructureSection load='1kq2' size='340' side='right'caption='[[1kq2]], [[Resolution|resolution]] 2.71Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1kq2]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1kq2]] is a 7 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KQ2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.71Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kq2 OCA], [https://pdbe.org/1kq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kq2 RCSB], [https://www.ebi.ac.uk/pdbsum/1kq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kq2 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kq2 OCA], [https://pdbe.org/1kq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kq2 RCSB], [https://www.ebi.ac.uk/pdbsum/1kq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kq2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A0A0H3JV59_STAAM A0A0H3JV59_STAAM] RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.[HAMAP-Rule:MF_00436] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 36: | Line 36: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Brennan | [[Category: Staphylococcus aureus]] | ||
[[Category: Moller | [[Category: Brennan RG]] | ||
[[Category: Pearson | [[Category: Moller T]] | ||
[[Category: Schumacher | [[Category: Pearson RF]] | ||
[[Category: Valentin-Hansen | [[Category: Schumacher MA]] | ||
[[Category: Valentin-Hansen P]] | |||
Latest revision as of 12:02, 16 August 2023
Crystal Structure of an Hfq-RNA ComplexCrystal Structure of an Hfq-RNA Complex
Structural highlights
FunctionA0A0H3JV59_STAAM RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.[HAMAP-Rule:MF_00436] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||