4f7r: Difference between revisions
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==Crystal structure of 14-3-3 protein from Giardia intestinalis== | |||
<StructureSection load='4f7r' size='340' side='right' caption='[[4f7r]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4f7r]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Giain Giain]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F7R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F7R FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4f7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f7r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f7r RCSB], [http://www.ebi.ac.uk/pdbsum/4f7r PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 14-3-3s are a family of dimeric evolutionary conserved pSer/pThr binding proteins that play a key role in multiple biological processes by interacting with a plethora of client proteins. Giardia duodenalis is a flagellated protozoan that affects millions of people worldwide causing an acute and chronic diarrheal disease. The single giardial 14-3-3 isoform (g14-3-3), unique in the 14-3-3 family, needs the constitutive phosphorylation of Thr214 and the polyglycylation of its C-terminus to be fully functional in vivo. Alteration of the phosphorylation and polyglycylation status affects the parasite differentiation into the cyst stage. To further investigate the role of these post-translational modifications, the crystal structure of the g14-3-3 was solved in the unmodified apo form. Oligomers of g14-3-3 were observed due to domain swapping events at the protein C-terminus. The formation of filaments was supported by TEM. Mutational analysis, in combination with native PAGE and chemical cross-linking, proved that polyglycylation prevents oligomerization. In silico phosphorylation and molecular dynamics simulations supported a structural role for the phosphorylation of Thr214 in promoting target binding. Our findings highlight unique structural features of g14-3-3 opening novel perspectives on the evolutionary history of this protein family and envisaging the possibility to develop anti-giardial drugs targeting g14-3-3. | |||
The Crystal Structure of Giardia duodenalis 14-3-3 in the Apo Form: When Protein Post-Translational Modifications Make the Difference.,Fiorillo A, di Marino D, Bertuccini L, Via A, Pozio E, Camerini S, Ilari A, Lalle M PLoS One. 2014 Mar 21;9(3):e92902. doi: 10.1371/journal.pone.0092902. eCollection, 2014. PMID:24658679<ref>PMID:24658679</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
==See Also== | |||
*[[14-3-3 protein|14-3-3 protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Giain]] | [[Category: Giain]] | ||
[[Category: Fiorillo, A | [[Category: Fiorillo, A]] | ||
[[Category: Ilari, I | [[Category: Ilari, I]] | ||
[[Category: Lalle, M | [[Category: Lalle, M]] | ||
[[Category: 9-alpha-helix]] | [[Category: 9-alpha-helix]] | ||
[[Category: Homodimer]] | [[Category: Homodimer]] | ||
[[Category: Signal transduction]] | [[Category: Signal transduction]] | ||
[[Category: Signaling protein]] | [[Category: Signaling protein]] | ||
