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| | <StructureSection load='4mml' size='340' side='right'caption='[[4mml]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4mml' size='340' side='right'caption='[[4mml]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4mml]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MML FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4mml]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MML FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.801Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u1s|1u1s]], [[3inz|3inz]], [[3m4g|3m4g]], [[4mmk|4mmk]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hfq, PA4944 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=4mml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mml OCA], [https://pdbe.org/4mml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mml RCSB], [https://www.ebi.ac.uk/pdbsum/4mml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mml 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=4mml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mml OCA], [http://pdbe.org/4mml PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mml RCSB], [http://www.ebi.ac.uk/pdbsum/4mml PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mml ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HFQ_PSEAE HFQ_PSEAE]] 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). | + | [https://www.uniprot.org/uniprot/HFQ_PSEAE HFQ_PSEAE] 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). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4mml" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4mml" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Protein Hfq 3D structures|Protein Hfq 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Filimonov, V V]] | + | [[Category: Filimonov VV]] |
| - | [[Category: Melnik, B S]] | + | [[Category: Melnik BS]] |
| - | [[Category: Mueller, U]] | + | [[Category: Mueller U]] |
| - | [[Category: Murina, V N]] | + | [[Category: Murina VN]] |
| - | [[Category: Nikulin, A D]] | + | [[Category: Nikulin AD]] |
| - | [[Category: Uhlein, M]] | + | [[Category: Uhlein M]] |
| - | [[Category: Weiss, M]] | + | [[Category: Weiss M]] |
| - | [[Category: Lsm fold]]
| + | |
| - | [[Category: Rna binding protein]]
| + | |
| Structural highlights
Function
HFQ_PSEAE 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).
Publication Abstract from PubMed
Hfq is a thermostable RNA-binding bacterial protein that forms a uniquely shaped homohexamer. Based on sequence and structural similarity, Hfq belongs to the like-Sm (LSm) protein family. In spite of a rather high degree of homology between archaeal and eukaryotic LSm proteins, their quaternary structure is different, usually consisting of five to eight monomers. In this work, the importance of conserved intersubunit hydrogen bonds for the Hfq spatial organization was tested. The structures and stabilities for the Gln8Ala, Asn28Ala, Asp40Ala, and Tyr55Ala Hfq mutants were determined. All these proteins have the same hexamer organization, but their stability is different. Elimination of a single intersubunit hydrogen bond due to Gln8Ala, Asp40Ala, and Tyr55Ala substitutions results in decreased stability of the Hfq hexamer. Tyr55Ala Hfq as well as the earlier studied His57Ala Hfq has reduced protein thermostability, which seems to correspond to an opening of the protein hydrophobic core.
Effect of conserved intersubunit amino Acid substitutions on hfq protein structure and stability.,Murina VN, Melnik BS, Filimonov VV, Uhlein M, Weiss MS, Muller U, Nikulin AD Biochemistry (Mosc). 2014 May;79(5):469-77. doi: 10.1134/S0006297914050113. PMID:24954598[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Murina VN, Melnik BS, Filimonov VV, Uhlein M, Weiss MS, Muller U, Nikulin AD. Effect of conserved intersubunit amino Acid substitutions on hfq protein structure and stability. Biochemistry (Mosc). 2014 May;79(5):469-77. doi: 10.1134/S0006297914050113. PMID:24954598 doi:http://dx.doi.org/10.1134/S0006297914050113
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