1kq1
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1kq1' size='340' side='right'caption='[[1kq1]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='1kq1' size='340' side='right'caption='[[1kq1]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1kq1]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1kq1]] is a 12 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=1KQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KQ1 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]] 1.55Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></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=1kq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kq1 OCA], [https://pdbe.org/1kq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kq1 RCSB], [https://www.ebi.ac.uk/pdbsum/1kq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kq1 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=1kq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kq1 OCA], [https://pdbe.org/1kq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kq1 RCSB], [https://www.ebi.ac.uk/pdbsum/1kq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kq1 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 20: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kq1 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kq1 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | |||
| - | 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<ref>PMID:12093755</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1kq1" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Protein Hfq|Protein Hfq]] | + | *[[Protein Hfq 3D structures|Protein Hfq 3D structures]] |
| - | + | ||
| - | + | ||
__TOC__ | __TOC__ | ||
</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]] | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
1.55 A Crystal structure of the pleiotropic translational regulator, Hfq
| |||||||||||
