Ontology highlight
ABSTRACT:
SUBMITTER: Davenport AM
PROVIDER: S-EPMC4259157 | biostudies-literature | 2014 Jul
REPOSITORIES: biostudies-literature
Davenport Andrew M AM Collins Leslie N LN Chiu Hui H Minor Paul J PJ Sternberg Paul W PW Hoelz André A
Journal of molecular biology 20140517 14
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 r ...[more]