› 3tii

X-ray diffraction
2.5Å resolution

Tubulin tyrosine ligase

Released:
DOI: 10.2210/pdb3tii/pdb
PDB entry 3tii coloured by chain, front view.
PDB entry 3tii coloured by chain, side view.
PDB entry 3tii coloured by chain, top view.
Source organism: Xenopus tropicalis
Primary publication:
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 18 1250-8 (2011)
PMID: 22020298

Function and Biology Details

Reaction catalysed: 
ATP + detyrosinated alpha-tubulin + L-tyrosine = alpha-tubulin + ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123656 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tubulin--tyrosine ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 380 amino acids
Theoretical weight: 43.74 KDa
Source organism: Xenopus tropicalis
Expression system: Escherichia coli
UniProt:
  • Canonical: F6Z895 (Residues: 2-377; Coverage: 100%)
Gene name: ttl
Sequence domains: Tubulin-tyrosine ligase family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ANP 2 x ANP
Ligand MG 7 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 44.416Å b: 74.663Å c: 117.328Å
α: 90° β: 90.11° γ: 90°
R-values:
R R work R free
0.254 0.254 0.285
Expression system: Escherichia coli

Quick links

Citations

24 review citations

The tubulin code: molecular components, readout mechanisms, and functions.
Janke C. (2014)
23 more

2 mentions without citation

Structural basis of tubulin tyrosination by tubulin tyrosine ligase.
Prota et al. (2013)
1 more