5vlq

Structure of the TTLL3 Glycylase

spinqualitylabelsall models 5vlq, resolution 2.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vlq is a 2 chain structure with sequence from Xenopus tropicalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.285Å Ligands: ANP, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TTLL3_XENTR Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin. Not involved in elongation step of the polyglycylation reaction (PubMed:28576883). Preferentially glycylates a beta-tail peptide over the alpha-tail, although shifts its preference toward alpha-tail as beta-tail glutamylation increases (PubMed:28576883). Competes with polyglutamylases for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (PubMed:28576883). Together with TTLL8, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance (By similarity).[UniProtKB:A4Q9E5]

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