8U3Z
Model of TTLL6 bound to microtubule from composite map
Summary for 8U3Z
| Entry DOI | 10.2210/pdb8u3z/pdb |
| Related | 8T42 |
| EMDB information | 41090 |
| Descriptor | Tubulin alpha-1B chain, Tubulin beta chain, Tubulin polyglutamylase TTLL6, ... (7 entities in total) |
| Functional Keywords | tubulin, post-translational modifications, microtubules, tubulin tyrosine ligase like family enzymes, ligase |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 5 |
| Total formula weight | 297162.82 |
| Authors | Mahalingan, K.K.,Grotjahn, D.,Li, Y.,Lander, G.C.,Zehr, E.A.,Roll-Mecak, A. (deposition date: 2023-09-08, release date: 2024-05-29) |
| Primary citation | Mahalingan, K.K.,Grotjahn, D.A.,Li, Y.,Lander, G.C.,Zehr, E.A.,Roll-Mecak, A. Structural basis for alpha-tubulin-specific and modification state-dependent glutamylation. Nat.Chem.Biol., 2024 Cited by PubMed Abstract: Microtubules have spatiotemporally complex posttranslational modification patterns. Tubulin tyrosine ligase-like (TTLL) enzymes introduce the most prevalent modifications on α-tubulin and β-tubulin. How TTLLs specialize for specific substrate recognition and ultimately modification-pattern generation is largely unknown. TTLL6, a glutamylase implicated in ciliopathies, preferentially modifies tubulin α-tails in microtubules. Cryo-electron microscopy, kinetic analysis and single-molecule biochemistry reveal an unprecedented quadrivalent recognition that ensures simultaneous readout of microtubule geometry and posttranslational modification status. By binding to a β-tubulin subunit, TTLL6 modifies the α-tail of the longitudinally adjacent tubulin dimer. Spanning two tubulin dimers along and across protofilaments (PFs) ensures fidelity of recognition of both the α-tail and the microtubule. Moreover, TTLL6 reads out and is stimulated by glutamylation of the β-tail of the laterally adjacent tubulin dimer, mediating crosstalk between α-tail and β-tail. This positive feedback loop can generate localized microtubule glutamylation patterns. Our work uncovers general principles that generate tubulin chemical and topographic complexity. PubMed: 38658656DOI: 10.1038/s41589-024-01599-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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