View source for 4icu


==Ubiquitin-like domain of human tubulin folding cofactor E - crystal from A==
<StructureSection load='4icu' size='340' side='right'caption='[[4icu]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4icu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ICU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ICU 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]] 2.4&#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=4icu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4icu OCA], [https://pdbe.org/4icu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4icu RCSB], [https://www.ebi.ac.uk/pdbsum/4icu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4icu ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/TBCE_HUMAN TBCE_HUMAN] Sanjad-Sakati syndrome;Autosomal recessive Kenny-Caffey syndrome. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/TBCE_HUMAN TBCE_HUMAN] Tubulin-folding protein; involved in the second step of the tubulin folding pathway. Seems to be implicated in the maintenance of the neuronal microtubule network. Involved in regulation of tubulin heterodimer dissociation.<ref>PMID:11847227</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tubulin proteostasis is regulated by a group of molecular chaperones termed tubulin cofactors (TBC). Whereas tubulin heterodimer formation is well-characterized biochemically, its dissociation pathway is not clearly understood. Here, we carried out biochemical assays to dissect the role of the human TBCE and TBCB chaperones in alpha-tubulin-beta-tubulin dissociation. We used electron microscopy and image processing to determine the three-dimensional structure of the human TBCE, TBCB and alpha-tubulin (alphaEB) complex, which is formed upon alpha-tubulin-beta-tubulin heterodimer dissociation by the two chaperones. Docking the atomic structures of domains of these proteins, including the TBCE UBL domain, as we determined by X-ray crystallography, allowed description of the molecular architecture of the alphaEB complex. We found that heterodimer dissociation is an energy-independent process that takes place through a disruption of the alpha-tubulin-beta-tubulin interface that is caused by a steric interaction between beta-tubulin and the TBCE cytoskeleton-associated protein glycine-rich (CAP-Gly) and leucine-rich repeat (LRR) domains. The protruding arrangement of chaperone ubiquitin-like (UBL) domains in the alphaEB complex suggests that there is a direct interaction of this complex with the proteasome, thus mediating alpha-tubulin degradation.

The structure of the complex between alpha-tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanism.,Serna M, Carranza G, Martin-Benito J, Janowski R, Canals A, Coll M, Zabala JC, Valpuesta JM J Cell Sci. 2015 May 1;128(9):1824-34. doi: 10.1242/jcs.167387. Epub 2015 Apr 23. PMID:25908846<ref>PMID:25908846</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4icu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Boutin M]]
[[Category: Coll M]]
[[Category: Janowski R]]
[[Category: Zabala JC]]