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== | ==Hfq protein from Pseudomonas aeruginosa. Low-salt crystals== | ||
<StructureSection load='1u1s' size='340' side='right'caption='[[1u1s]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1u1s]] 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=1U1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U1S FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</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=1u1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u1s OCA], [https://pdbe.org/1u1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u1s RCSB], [https://www.ebi.ac.uk/pdbsum/1u1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u1s ProSAT], [https://www.topsan.org/Proteins/RSGI/1u1s TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u1/1u1s_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1u1s ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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. | 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<ref>PMID:15681864</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1u1s" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Protein Hfq|Protein Hfq]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Blaesi U]] | |||
[[Category: Blaesi | [[Category: Garber M]] | ||
[[Category: Garber | [[Category: Kachalova G]] | ||
[[Category: Kachalova | [[Category: Moll I]] | ||
[[Category: Moll | [[Category: Nikonov SV]] | ||
[[Category: Nikonov | [[Category: Nikulin AD]] | ||
[[Category: Nikulin | [[Category: Perederina I]] | ||
[[Category: Perederina | [[Category: Stolboushkina EA]] | ||
[[Category: Vassilieva IM]] | |||
[[Category: Stolboushkina | [[Category: Vassylyev D]] | ||
[[Category: Vassilieva | [[Category: Yokoyama S]] | ||
[[Category: Vassylyev | |||
[[Category: Yokoyama | |||
Latest revision as of 09:36, 23 August 2023
Hfq protein from Pseudomonas aeruginosa. Low-salt crystalsHfq protein from Pseudomonas aeruginosa. Low-salt crystals
Structural highlights
FunctionHFQ_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 PubMedThe 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 AlsoReferences
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