4IF5

Structure of human Mec17

4IF5 の概要

• エントリーDOI: 10.2210/pdb4if5/pdb
• 関連するPDBエントリー: 4I9Y 4IF6 4IG9
• 分子名称: Alpha-tubulin N-acetyltransferase, ACETYL COENZYME *A, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: acetyltransferase, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q5SQI0
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23488.34

構造登録者

Davenport, A.M.,Collins, L.,Minor, P.,Sternberg, P.,Hoelz, A. (登録日: 2012-12-14, 公開日: 2014-05-28, 最終更新日: 2024-10-16)

主引用文献

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

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: 24846647
DOI: 10.1016/j.jmb.2014.05.009

実験手法

X-RAY DIFFRACTION (1.7 Å)