4IF5
Structure of human Mec17
Summary for 4IF5
| Entry DOI | 10.2210/pdb4if5/pdb |
| Related | 4I9Y 4IF6 4IG9 |
| Descriptor | Alpha-tubulin N-acetyltransferase, ACETYL COENZYME *A, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | acetyltransferase, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q5SQI0 |
| Total number of polymer chains | 1 |
| Total formula weight | 23488.34 |
| Authors | Davenport, A.M.,Collins, L.,Minor, P.,Sternberg, P.,Hoelz, A. (deposition date: 2012-12-14, release date: 2014-05-28, Last modification date: 2024-10-16) |
| Primary citation | Davenport, A.M.,Collins, L.N.,Chiu, H.,Minor, P.J.,Sternberg, P.W.,Hoelz, A. Structural and Functional Characterization of the alpha-Tubulin Acetyltransferase MEC-17. J.Mol.Biol., 426:2605-2616, 2014 Cited by PubMed Abstract: Tubulin protomers undergo an extensive array of post-translational modifications to tailor microtubules to specific tasks. One such modification, the acetylation of lysine 40 of α-tubulin, located in the lumen of microtubules, is associated with stable, long-living microtubule structures. MEC-17 was recently identified as the acetyltransferase that mediates this event. We have determined the crystal structure of the catalytic core of human MEC-17 in complex with its cofactor acetyl-CoA at 1.7Å resolution. The structure reveals that the MEC-17 core adopts a canonical Gcn5-related N-acetyltransferase (GNAT) fold that is decorated with extensive surface loops. An enzymatic analysis of 33 MEC-17 surface mutants identifies hot-spot residues for catalysis and substrate recognition. A large, evolutionarily conserved hydrophobic surface patch that is critical for enzymatic activity is identified, suggesting that specificity is achieved by interactions with the α-tubulin substrate that extend outside of the modified surface loop. An analysis of MEC-17 mutants in Caenorhabditis elegans shows that enzymatic activity is dispensable for touch sensitivity. PubMed: 24846647DOI: 10.1016/j.jmb.2014.05.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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