4if5

Structure of human Mec17

spinqualitylabelsall models 4if5, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4if5 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACO, CL NonStd Res: MSE Related: 4i9y, 4if6, 4ig9 Activity: Alpha-tubulin N-acetyltransferase, with EC number 2.3.1.108 Resources: FirstGlance, OCA, RCSB, PDBsum Function [ATAT_HUMAN] Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. May affect microtubule stability and regulate microtubule dynamics. May be involved in neuron development. Publication Abstract from PubMed 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 alpha-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 1.7A 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 alpha-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. Structural and Functional Characterization of the alpha-Tubulin Acetyltransferase MEC-17.,Davenport AM, Collins LN, Chiu H, Minor PJ, Sternberg PW, Hoelz A J Mol Biol. 2014 Jul 15;426(14):2605-16. doi: 10.1016/j.jmb.2014.05.009. Epub, 2014 May 17. PMID:24846647 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA