3qsu: Difference between revisions
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==Structure of Staphylococcus aureus Hfq in complex with A7 RNA== | |||
=== | <StructureSection load='3qsu' size='340' side='right' caption='[[3qsu]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3qsu]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_ect-r_2 Staphylococcus aureus subsp. aureus ect-r 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QSU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QSU FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gib|3gib]], [[1kq1|1kq1]], [[1kq2|1kq2]], [[3hsb|3hsb]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECTR2_1161, hfq ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=889933 Staphylococcus aureus subsp. aureus ECT-R 2])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qsu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qsu RCSB], [http://www.ebi.ac.uk/pdbsum/3qsu PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Hfq is a post-transcriptional regulator that plays a key role in bacterial gene expression by binding AU-rich sequences and A-tracts to facilitate the annealing of sRNAs to target mRNAs and to affect RNA stability. To understand how Hfq from the Gram-positive bacterium Staphylococcus aureus (Sa) binds A-tract RNA, we determined the crystal structure of an Sa Hfq-adenine oligoribonucleotide complex. The structure reveals a bipartite RNA-binding motif on the distal face that is composed of a purine nucleotide-specificity site (R-site) and a non-discriminating linker site (L-site). The (R-L)-binding motif, which is also utilized by Bacillus subtilis Hfq to bind (AG)(3)A, differs from the (A-R-N) tripartite poly(A) RNA-binding motif of Escherichia coli Hfq whereby the Sa Hfq R-site strongly prefers adenosine, is more aromatic and permits deeper insertion of the adenine ring. R-site adenine-stacking residue Phe30, which is conserved among Gram-positive bacterial Hfqs, and an altered conformation about beta3 and beta4 eliminate the adenosine-specificity site (A-site) and create the L-site. Binding studies show that Sa Hfq binds (AU)(3)A approximately (AG)(3)A >/= (AC)(3)A > (AA)(3)A and L-site residue Lys33 plays a significant role. The (R-L) motif is likely utilized by Hfqs from most Gram-positive bacteria to bind alternating (A-N)(n) RNA. | |||
Structural mechanism of Staphylococcus aureus Hfq binding to an RNA A-tract.,Horstmann N, Orans J, Valentin-Hansen P, Shelburne SA 3rd, Brennan RG Nucleic Acids Res. 2012 Sep 10. PMID:22965117<ref>PMID:22965117</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Staphylococcus aureus subsp. aureus ect-r 2]] | [[Category: Staphylococcus aureus subsp. aureus ect-r 2]] | ||
[[Category: Brennan, R | [[Category: Brennan, R]] | ||
[[Category: Horstmann, N | [[Category: Horstmann, N]] | ||
[[Category: Link, T M | [[Category: Link, T M]] | ||
[[Category: Chaperone-rna complex]] | [[Category: Chaperone-rna complex]] | ||
[[Category: Cytoplasma]] | [[Category: Cytoplasma]] | ||
