View source for 5lvz


==Crystal structure of yeast 14-3-3 protein from Lachancea thermotolerans==
<StructureSection load='5lvz' size='340' side='right'caption='[[5lvz]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lvz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lachancea_thermotolerans_CBS_6340 Lachancea thermotolerans CBS 6340]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5lho 5lho]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LVZ 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]] 1.95&#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=5lvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lvz OCA], [https://pdbe.org/5lvz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lvz RCSB], [https://www.ebi.ac.uk/pdbsum/5lvz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lvz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C5DN49_LACTC C5DN49_LACTC] 
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== Publication Abstract from PubMed ==
14-3-3 proteins bind phosphorylated binding partners to regulate several of their properties, including enzymatic activity, stability and subcellular localization. Here, two crystal structures are presented: the crystal structures of the 14-3-3 protein (also known as Bmh1) from the yeast Lachancea thermotolerans in the unliganded form and bound to a phosphopeptide derived from human PI4KB (phosphatidylinositol 4-kinase B). The structures demonstrate the high evolutionary conservation of ligand recognition by 14-3-3 proteins. The structural analysis suggests that ligand recognition by 14-3-3 proteins evolved very early in the evolution of eukaryotes and remained conserved, underlying the importance of 14-3-3 proteins in physiology.

Crystal structures of a yeast 14-3-3 protein from Lachancea thermotolerans in the unliganded form and bound to a human lipid kinase PI4KB-derived peptide reveal high evolutionary conservation.,Eisenreichova A, Klima M, Boura E Acta Crystallogr F Struct Biol Commun. 2016 Nov 1;72(Pt 11):799-803. Epub 2016, Oct 24. PMID:27827352<ref>PMID:27827352</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lvz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Lachancea thermotolerans CBS 6340]]
[[Category: Large Structures]]
[[Category: Boura E]]
[[Category: Klima M]]