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| ==Crystal Structure of Escherichia coli Hfq Proximal Pore Mutant== | | ==Crystal Structure of Escherichia coli Hfq Proximal Pore Mutant== |
| <StructureSection load='4jli' size='340' side='right' caption='[[4jli]], [[Resolution|resolution]] 1.79Å' scene=''> | | <StructureSection load='4jli' size='340' side='right'caption='[[4jli]], [[Resolution|resolution]] 1.79Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4jli]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JLI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JLI FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4jli]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JLI FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jri|4jri]], [[4jrk|4jrk]]</td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hfq, O3O_02600 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=4jli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jli OCA], [https://pdbe.org/4jli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jli RCSB], [https://www.ebi.ac.uk/pdbsum/4jli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jli ProSAT]</span></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=4jli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jli OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jli RCSB], [http://www.ebi.ac.uk/pdbsum/4jli PDBsum]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Hfq is a posttranscriptional riboregulator and RNA chaperone that binds small RNAs and target mRNAs to effect their annealing and message-specific regulation in response to environmental stressors. Structures of Hfq-RNA complexes indicate that U-rich sequences prefer the proximal face and A-rich sequences the distal face; however, the Hfq-binding sites of most RNAs are unknown. Here, we present an Hfq-RNA mapping approach that uses single tryptophan-substituted Hfq proteins, all of which retain the wild-type Hfq structure, and tryptophan fluorescence quenching (TFQ) by proximal RNA binding. TFQ properly identified the respective distal and proximal binding of A15 and U6 RNA to Gram-negative Escherichia coli (Ec) Hfq and the distal face binding of (AA)3A, (AU)3A and (AC)3A to Gram-positive Staphylococcus aureus (Sa) Hfq. The inability of (GU)3G to bind the distal face of Sa Hfq reveals the (R-L)n binding motif is a more restrictive (A-L)n binding motif. Remarkably Hfq from Gram-positive Listeria monocytogenes (Lm) binds (GU)3G on its proximal face. TFQ experiments also revealed the Ec Hfq (A-R-N)n distal face-binding motif should be redefined as an (A-A-N)n binding motif. TFQ data also demonstrated that the 5'-untranslated region of hfq mRNA binds both the proximal and distal faces of Ec Hfq and the unstructured C-terminus.
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| Mapping Hfq-RNA interaction surfaces using tryptophan fluorescence quenching.,Robinson KE, Orans J, Kovach AR, Link TM, Brennan RG Nucleic Acids Res. 2013 Nov 27. PMID:24288369<ref>PMID:24288369</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| | ==See Also== |
| </div>
| | *[[Protein Hfq 3D structures|Protein Hfq 3D structures]] |
| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacillus coli migula 1895]] | | [[Category: Escherichia coli]] |
| [[Category: Orans, J]] | | [[Category: Large Structures]] |
| [[Category: Robinson, K E]] | | [[Category: Orans J]] |
| [[Category: Post-transcriptional regulator]] | | [[Category: Robinson KE]] |
| [[Category: Riboregulator]]
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| [[Category: Rna binding protein]]
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