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5vlq
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the TTLL3 Glycylase== | |
| - | + | <StructureSection load='5vlq' size='340' side='right'caption='[[5vlq]], [[Resolution|resolution]] 2.29Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5vlq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_tropicalis Xenopus tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VLQ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.285Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5vlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vlq OCA], [https://pdbe.org/5vlq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vlq RCSB], [https://www.ebi.ac.uk/pdbsum/5vlq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vlq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TTLL3_XENTR 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]<ref>PMID:28576883</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Xenopus tropicalis]] | ||
| + | [[Category: Garnham CP]] | ||
| + | [[Category: Li Y]] | ||
| + | [[Category: Roll-Mecak A]] | ||
| + | [[Category: Yu I]] | ||
Current revision
Structure of the TTLL3 Glycylase
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