Tubulin acetyltransferase

spinqualitylabelsall models Se-Met human tubulin cetyltransferase complex with acetyl CoA and Cl- ion (green) (PDB code 4if5) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Tubulin acetyltransferase or alpha-tubulin N-acetyltransferase (TAT) is the major tubulin lysine-40 (K40) acetyltransferase. TAT catalyzes the conversion of acetyl-CoA and tubulin-L-lysine to CoA and tubulin-N-acetyl-L-lysine. The posttranslational modification of tubulin is essential for stable, long-lived micrutubules. This tubulin modification is conserved from prosits to humans. TAT accelerates microtubules dynamics via a mechanism distinct from acetylation. Relevance Depletion of TAT leads to a significant increase in the frequency of microtubule breakage. Abnormal levels of tubulin K40 acetylation is linked to neurological disorders, cancer and hear diseases. Structural highlights The acetyl-CoA donor is encapsulated in a highly conserved basic pocket on the surface of TAT forming numerous hydrogen bonds with TAT residues. Water moleculres are shown as red spheres. The donor acetyl group is oriented by a hydrogen bond with the backbone of F124 (colored in magenta) and is proximal to a groove which must bind the incoming K40 substrate of tubulin.

3D structures of tubulin acetyltransferase

Updated on 23-December-2020

4pk2, 4pk3 – hTAT catalytic domain + Acetyl CoA + bisubstrate analog - human
4gs4, 4b5o, 4u9y, 4u9z, 3vwe, 4if5 – hTAT catalytic domain + Acetyl CoA
4b5p – hTAT catalytic domain (mutant) + Acetyl CoA
3vwd – hTAT catalytic domain + acetoacetyl CoA
4h6z, 4hkf, 4yrh – zTAT + Acetyl CoA – zebrafish
4h6u – zTAT (mutant) + Acetyl CoA

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