3tii | pdb_00003tii

Tubulin tyrosine ligase

spinqualitylabelsall models 3tii, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tii is a 2 chain structure with sequence from Eukaryota. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANP, MG Related: 3tig, 3tin Gene: ttl (Eukaryota) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Tubulin tyrosine ligase (TTL) catalyzes the post-translational C-terminal tyrosination of alpha-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. Tubulin tyrosine ligase structure reveals adaptation of an ancient fold to bind and modify tubulin.,Szyk A, Deaconescu AM, Piszczek G, Roll-Mecak A Nat Struct Mol Biol. 2011 Oct 23;18(11):1250-8. doi: 10.1038/nsmb.2148. PMID:22020298 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA