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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://pdbe.org/4jli PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jli RCSB], [http://www.ebi.ac.uk/pdbsum/4jli PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jli ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function ==
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| [[http://www.uniprot.org/uniprot/K0BDC5_ECO1E K0BDC5_ECO1E]] 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 (By similarity).[HAMAP-Rule:MF_00436][SAAS:SAAS005001_004_036087]
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| <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>
| | ==See Also== |
| | | *[[Protein Hfq 3D structures|Protein Hfq 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4jli" style="background-color:#fffaf0;"></div>
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| == 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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