8YAR
ATAT-2 bound K40R MEC-12/MEC-7 microtubule
Summary for 8YAR
| Entry DOI | 10.2210/pdb8yar/pdb |
| EMDB information | 39105 |
| Descriptor | Tubulin alpha-3 chain, Alpha-tubulin N-acetyltransferase 2, Tubulin beta-1 chain, ... (6 entities in total) |
| Functional Keywords | microtubules, luminal enzymes, ptms, structural protein |
| Biological source | Caenorhabditis elegans More |
| Total number of polymer chains | 6 |
| Total formula weight | 262768.88 |
| Authors | |
| Primary citation | Luo, J.,Lam, W.H.,Yu, D.,Chao, V.C.,Zopfi, M.N.,Khoo, C.J.,Zhao, C.,Yan, S.,Liu, Z.,Li, X.D.,Zheng, C.,Zhai, Y.,Ti, S.C. Tubulin acetyltransferases access and modify the microtubule luminal K40 residue through anchors in taxane-binding pockets. Nat.Struct.Mol.Biol., 32:358-368, 2025 Cited by PubMed Abstract: Acetylation at α-tubulin K40 is the sole post-translational modification preferred to occur inside the lumen of hollow cylindrical microtubules. However, how tubulin acetyltransferases access the luminal K40 in micrometer-long microtubules remains unknown. Here, we use cryo-electron microscopy and single-molecule reconstitution assays to reveal the enzymatic mechanism for tubulin acetyltransferases to modify K40 in the lumen. One tubulin acetyltransferase spans across the luminal lattice, with the catalytic core docking onto two α-tubulins and the enzyme's C-terminal domain occupying the taxane-binding pockets of two β-tubulins. The luminal accessibility and enzyme processivity of tubulin acetyltransferases are inhibited by paclitaxel, a microtubule-stabilizing chemotherapeutic agent. Characterizations using recombinant tubulins mimicking preacetylated and postacetylated K40 show the crosstalk between microtubule acetylation states and the cofactor acetyl-CoA in enzyme turnover. Our findings provide crucial insights into the conserved multivalent interactions involving α- and β-tubulins to acetylate the confined microtubule lumen. PubMed: 39496813DOI: 10.1038/s41594-024-01406-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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