4icu

Ubiquitin-like domain of human tubulin folding cofactor E - crystal from A

spinqualitylabelsall models 4icu, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4icu is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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