5vlq: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 5vlq is ~~ON HOLD~~

==Structure of the TTLL3 Glycylase==

~~Authors~~:

== 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 guided tour on the structure components use [https://proteopedia.org/fgij/fg.htm?mol=5VLQ FirstGlance].

~~Description~~:

</td></tr><tr id='method'><td class="sblockLbl">[[Empirical_models|Method:]]</td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.285Å</td></tr>

[[Category: ~~Unreleased~~ Structures]]

<tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</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">Resources:</td><td class="sblockDat">[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]</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 ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Xenopus tropicalis]]

[[Category: Garnham CP]]

[[Category: Li Y]]

[[Category: Roll-Mecak A]]

[[Category: Yu I]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5vlq is ON HOLD
+==Structure of the TTLL3 Glycylase==
+<StructureSection load='5vlq' size='340' side='right'caption='[[5vlq]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
-Authors:
+== 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>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.285&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<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]]