3TIN

Tubulin tyrosine ligase

3TIN の概要

• エントリーDOI: 10.2210/pdb3tin/pdb
• 関連するPDBエントリー: 3TIG 3TII
• 分子名称: Ttl protein, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: atp-grasp, ligase, tubulin, tyrosination
• 由来する生物種: Xenopus (Silurana) tropicalis (Western clawed frog)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44239.65

構造登録者

Roll-Mecak, A.,Szyk, A.,Deaconescu, A.,Piszczek, G. (登録日: 2011-08-20, 公開日: 2011-10-26, 最終更新日: 2024-02-28)

主引用文献

Szyk, A.,Deaconescu, A.M.,Piszczek, G.,Roll-Mecak, A.
Tubulin tyrosine ligase structure reveals adaptation of an ancient fold to bind and modify tubulin.
Nat.Struct.Mol.Biol., 18:1250-1258, 2011

PubMed Abstract: Tubulin tyrosine ligase (TTL) catalyzes the post-translational C-terminal tyrosination of α-tubulin. Tyrosination regulates recruitment of microtubule-interacting proteins. TTL is essential. Its loss causes morphogenic abnormalities and is associated with cancers of poor prognosis. We present the first crystal structure of TTL (from Xenopus tropicalis), defining the structural scaffold upon which the diverse TTL-like family of tubulin-modifying enzymes is built. TTL recognizes tubulin using a bipartite strategy. It engages the tubulin tail through low-affinity, high-specificity interactions, and co-opts what is otherwise a homo-oligomerization interface in structurally related ATP grasp-fold enzymes to form a tight hetero-oligomeric complex with the tubulin body. Small-angle X-ray scattering and functional analyses reveal that TTL forms an elongated complex with the tubulin dimer and prevents its incorporation into microtubules by capping the tubulin longitudinal interface, possibly modulating the partition of tubulin between monomeric and polymeric forms.

PubMed: 22020298
DOI: 10.1038/nsmb.2148

実験手法

X-RAY DIFFRACTION (2.9 Å)