5LVZ

Crystal structure of yeast 14-3-3 protein from Lachancea thermotolerans

Replaces:  5LHO

Summary for 5LVZ

• Entry DOI: 10.2210/pdb5lvz/pdb
• Descriptor: KLTH0G14146p (2 entities in total)
• Functional Keywords: 14-3-3, signaling protein
• Biological source: Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
• Total number of polymer chains: 1
• Total formula weight: 28603.86

Authors

Klima, M.,Boura, E. (deposition date: 2016-09-14, release date: 2016-10-19, Last modification date: 2024-01-17)

Primary citation

Eisenreichova, A.,Klima, M.,Boura, E.
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.
Acta Crystallogr.,Sect.F, 72:799-803, 2016

PubMed Abstract: 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.

PubMed: 27827352
DOI: 10.1107/S2053230X16015053

Experimental method

X-RAY DIFFRACTION (1.95 Å)