View source for 5mkl


==Crystal structure of SmAP (LSm) protein from Sulfolobus acidocaldarius==
<StructureSection load='5mkl' size='340' side='right'caption='[[5mkl]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mkl]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MKL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MKL 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]] 2.086&#8491;</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=5mkl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mkl OCA], [https://pdbe.org/5mkl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mkl RCSB], [https://www.ebi.ac.uk/pdbsum/5mkl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mkl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0U3FHU0_9CREN A0A0U3FHU0_9CREN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sm and Sm-like (Lsm) proteins are considered as an evolutionary conserved family involved in RNA metabolism in organisms from bacteria and archaea to human. Currently, the function of Sm-like archaeal proteins (SmAP) is not well understood. Here, we report the crystal structures of SmAP proteins from Sulfolobus acidocaldarius and Methanococcus vannielii and a comparative analysis of their RNA-binding sites. Our data show that these SmAPs have only a uridine-specific RNA-binding site, unlike their bacterial homolog Hfq, which has three different RNA-binding sites. Moreover, variations in the amino acid composition of the U-binding sites of the two SmAPs lead to a difference in protein affinity for oligo(U) RNA. Surface plasmon resonance data and nucleotide-binding analysis confirm the high affinity of SmAPs for uridine nucleotides and oligo(U) RNA and the reduced affinity for adenines, guanines, cytidines and corresponding oligo-RNAs. In addition, we demonstrate that MvaSmAP1 and SacSmAP2 are capable of melting an RNA hairpin and, apparently, promote its interaction with complementary RNA.

Crystal structures and RNA-binding properties of Lsm proteins from archaea Sulfolobus acidocaldarius and Methanococcus vannielii: Similarity and difference of the U-binding mode.,Lekontseva N, Mikhailina A, Fando M, Kravchenko O, Balobanov V, Tishchenko S, Nikulin A Biochimie. 2020 Aug;175:1-12. doi: 10.1016/j.biochi.2020.05.001. Epub 2020 May, 15. PMID:32422160<ref>PMID:32422160</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5mkl" style="background-color:#fffaf0;"></div>

==See Also==
*[[Sm-like protein 3D structures|Sm-like protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sulfolobus acidocaldarius]]
[[Category: Lekontseva NV]]
[[Category: Nikulin AD]]
[[Category: Tishchenko SV]]