5cya

Crystal structure of Arl2 GTPase-activating protein tubulin cofactor C (TBCC)

spinqualitylabelsall models 5cya, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5cya is a 2 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Gene: CIN2, YPL241C, P1043 (Baker's yeast) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TBCC_YEAST] Tubulin-folding protein; involved in the early step of the tubulin folding pathway. Publication Abstract from PubMed Microtubule dynamics and polarity stem from the polymerization of alphass-tubulin heterodimers. Five conserved tubulin cofactors/chaperones and the Arl2 GTPase regulate alpha- and beta-tubulin assembly into heterodimers and maintain the soluble tubulin pool in the cytoplasm, but their physical mechanisms are unknown. Here, we reconstitute a core tubulin chaperone consisting of tubulin cofactors TBCD, TBCE and Arl2, and reveal a cage-like structure for regulating alphabeta-tubulin. Biochemical assays and electron microscopy structures of multiple intermediates show the sequential binding of alphabeta-tubulin dimer followed by tubulin cofactor TBCC onto this chaperone, forming a ternary complex in which Arl2 GTP hydrolysis is activated to alter alphabeta-tubulin conformation. A GTP-state locked Arl2 mutant inhibits ternary complex dissociation in vitro and causes severe defects in microtubule dynamics in vivo. Our studies suggest a revised paradigm for tubulin cofactors and Arl2 functions as a catalytic chaperone that regulates soluble alphabeta-tubulin assembly and maintenance to support microtubule dynamics. Tubulin cofactors and Arl2 are cage-like chaperones that regulate the soluble alphabeta-tubulin pool for microtubule dynamics.,Nithiananatham S, Le S, Seto E, Jia W, Leary J, Corbett KD, Moore JK, Al-Bassam J Elife. 2015 Jul 24;4. doi: 10.7554/eLife.08811. PMID:26208336 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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