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| | <StructureSection load='1u1t' size='340' side='right'caption='[[1u1t]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1u1t' size='340' side='right'caption='[[1u1t]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1u1t]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U1T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1U1T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1u1t]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U1T FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hk9|1hk9]], [[1qk1|1qk1]], [[1qk2|1qk2]], [[1u1s|1u1s]]</div></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]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hfq ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=1u1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u1t OCA], [https://pdbe.org/1u1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u1t RCSB], [https://www.ebi.ac.uk/pdbsum/1u1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u1t ProSAT], [https://www.topsan.org/Proteins/RSGI/1u1t TOPSAN]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1u1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u1t OCA], [http://pdbe.org/1u1t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u1t RCSB], [http://www.ebi.ac.uk/pdbsum/1u1t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u1t ProSAT], [http://www.topsan.org/Proteins/RSGI/1u1t TOPSAN]</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). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1u1t" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1u1t" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Protein Hfq|Protein Hfq]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Blaesi, U]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Garber, M]] | + | [[Category: Blaesi U]] |
| - | [[Category: Kachalova, G]] | + | [[Category: Garber M]] |
| - | [[Category: Moll, I]] | + | [[Category: Kachalova G]] |
| - | [[Category: Nikonov, S V]] | + | [[Category: Moll I]] |
| - | [[Category: Nikulin, A D]] | + | [[Category: Nikonov SV]] |
| - | [[Category: Perederina, A A]] | + | [[Category: Nikulin AD]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Perederina AA]] |
| - | [[Category: Stolboushkina, E A]] | + | [[Category: Stolboushkina EA]] |
| - | [[Category: Vassilieva, I M]] | + | [[Category: Vassilieva IM]] |
| - | [[Category: Vassylyev, D]] | + | [[Category: Vassylyev D]] |
| - | [[Category: Yokoyama, S]] | + | [[Category: Yokoyama S]] |
| - | [[Category: Hf1]]
| + | |
| - | [[Category: Hfq]]
| + | |
| - | [[Category: Rna binding protein]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Sm-like bacterial 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).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of the Hfq protein from Pseudomonas aeruginosa was determined using two different ionic conditions. In both cases the molecules formed identical hexameric rings, but some variations in the crystal packing were revealed. Hfq belongs to the family of Sm/LSm proteins, the members of which can form hexameric as well as heptameric rings. Comparative analysis of known structures of this protein family shows that the fragment of the Sm-fold responsible for oligomerization is strongly structurally conserved. In the heptameric ring, three conserved hydrogen bonds between beta-strands of adjacent molecules hold together the monomers, whereas in the hexameric rings of Hfq an additional conserved inaccessible hydrogen bond between neighbouring monomers is observed.
Structure of Pseudomonas aeruginosa Hfq protein.,Nikulin A, Stolboushkina E, Perederina A, Vassilieva I, Blaesi U, Moll I, Kachalova G, Yokoyama S, Vassylyev D, Garber M, Nikonov S Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):141-6. Epub 2005, Jan 19. PMID:15681864[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nikulin A, Stolboushkina E, Perederina A, Vassilieva I, Blaesi U, Moll I, Kachalova G, Yokoyama S, Vassylyev D, Garber M, Nikonov S. Structure of Pseudomonas aeruginosa Hfq protein. Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):141-6. Epub 2005, Jan 19. PMID:15681864 doi:10.1107/S0907444904030008
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