Structural highlights
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][1]
References
- ↑ Garnham CP, Yu I, Li Y, Roll-Mecak A. Crystal structure of tubulin tyrosine ligase-like 3 reveals essential architectural elements unique to tubulin monoglycylases. Proc Natl Acad Sci U S A. 2017 Jun 20;114(25):6545-6550. doi:, 10.1073/pnas.1617286114. Epub 2017 Jun 2. PMID:28576883 doi:http://dx.doi.org/10.1073/pnas.1617286114
