4x9d: Difference between revisions
New page: '''Unreleased structure''' The entry 4x9d is ON HOLD Authors: Nikulin, A.D, Tishchenko, S.V., Nikonova, E.Yu., Murina, V.N., Mihailina, A.O., Lekontseva, N.V. Description: High-resolut... |
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The | ==High-resolution structure of Hfq from Methanococcus jannaschii in complex with UMP== | ||
<StructureSection load='4x9d' size='340' side='right'caption='[[4x9d]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4x9d]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X9D 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]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</scene></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=4x9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x9d OCA], [https://pdbe.org/4x9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x9d RCSB], [https://www.ebi.ac.uk/pdbsum/4x9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x9d ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Y1435_METJA Y1435_METJA] | |||
<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> | |||
<div class="pdbe-citations 4x9d" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Protein Hfq 3D structures|Protein Hfq 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methanocaldococcus jannaschii]] | |||
[[Category: Lekontseva NV]] | |||
[[Category: Mihailina AO]] | |||
[[Category: Murina VN]] | |||
[[Category: Nikonova EY]] | |||
[[Category: Nikulin AD]] | |||
[[Category: Tishchenko SV]] | |||
Latest revision as of 13:47, 10 January 2024
High-resolution structure of Hfq from Methanococcus jannaschii in complex with UMPHigh-resolution structure of Hfq from Methanococcus jannaschii in complex with UMP
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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