|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='4icu' size='340' side='right'caption='[[4icu]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='4icu' size='340' side='right'caption='[[4icu]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4icu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ICU FirstGlance]. <br> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4icv|4icv]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TBCE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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> |
| - | <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=4icu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4icu OCA], [http://pdbe.org/4icu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4icu RCSB], [http://www.ebi.ac.uk/pdbsum/4icu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4icu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://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. | + | [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 == | | == Function == |
| - | [[http://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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 24: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boutin, M]] | + | [[Category: Boutin M]] |
| - | [[Category: Coll, M]] | + | [[Category: Coll M]] |
| - | [[Category: Janowski, R]] | + | [[Category: Janowski R]] |
| - | [[Category: Zabala, J C]] | + | [[Category: Zabala JC]] |
| - | [[Category: Alpha tubulin]]
| + | |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Tubulin folding cofactor]]
| + | |
| - | [[Category: Tubulin folding cofactor b]]
| + | |
| - | [[Category: Ubiquitin-like domain]]
| + | |
| Structural highlights
Disease
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
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bartolini F, Bhamidipati A, Thomas S, Schwahn U, Lewis SA, Cowan NJ. Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C. J Biol Chem. 2002 Apr 26;277(17):14629-34. Epub 2002 Feb 14. PMID:11847227 doi:10.1074/jbc.M200128200
- ↑ Serna M, Carranza G, Martin-Benito J, Janowski R, Canals A, Coll M, Zabala JC, Valpuesta JM. The structure of the complex between alpha-tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanism. J Cell Sci. 2015 May 1;128(9):1824-34. doi: 10.1242/jcs.167387. Epub 2015 Apr 23. PMID:25908846 doi:http://dx.doi.org/10.1242/jcs.167387
|
