5dy9: Difference between revisions
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The | ==Y68T Hfq from Methanococcus jannaschii in complex with AMP== | ||
<StructureSection load='5dy9' size='340' side='right' caption='[[5dy9]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dy9]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DY9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DY9 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x9c|4x9c]], [[4x9d|4x9d]], [[2qtx|2qtx]]</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=5dy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dy9 OCA], [http://pdbe.org/5dy9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dy9 RCSB], [http://www.ebi.ac.uk/pdbsum/5dy9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dy9 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Sm and Sm-like proteins are widely distributed among bacteria, archaea and eukarya. They participate in many processes related to RNA-processing and regulation of gene expression. While the function of the bacterial Lsm protein Hfq and eukaryotic Sm/Lsm proteins is rather well studied, the role of Lsm proteins in Archaea is investigated poorly. In this work, the RNA-binding ability of an archaeal Hfq-like protein from Methanococcus jannaschii has been studied by X-ray crystallography, anisotropy fluorescence and surface plasmon resonance. It has been found that MjaHfq preserves the proximal RNA-binding site that usually recognizes uridine-rich sequences. Distal adenine-binding and lateral RNA-binding sites show considerable structural changes as compared to bacterial Hfq. MjaHfq did not bind mononucleotides at these sites and would not recognize single-stranded RNA as its bacterial homologues. Nevertheless, MjaHfq possesses affinity to poly(A) RNA that seems to bind at the unstructured positive-charged N-terminal tail of the protein. | |||
Characterization of RNA-binding properties of the archaeal Hfq-like protein from Methanococcus jannaschii.,Nikulin A, Mikhailina A, Lekontseva N, Balobanov V, Nikonova E, Tishchenko S J Biomol Struct Dyn. 2016 Aug 1:1-14. PMID:27187760<ref>PMID:27187760</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: Balobanov, V | <div class="pdbe-citations 5dy9" style="background-color:#fffaf0;"></div> | ||
[[Category: Lekontseva, N | == References == | ||
[[Category: | <references/> | ||
[[Category: Nikonova, E | __TOC__ | ||
[[Category: Nikulin, A | </StructureSection> | ||
[[Category: | [[Category: Balobanov, V A]] | ||
[[Category: Lekontseva, N V]] | |||
[[Category: Mikhailina, A O]] | |||
[[Category: Nikonova, E Y]] | |||
[[Category: Nikulin, A D]] | |||
[[Category: Tishchenko, S V]] | |||
[[Category: Hfq]] | |||
[[Category: Lsm protein]] | |||
[[Category: Ribonucleotide-protein complex]] | |||
[[Category: Rna binding protein]] | |||
