This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5vlq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:11, 13 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5vlq' size='340' side='right'caption='[[5vlq]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
<StructureSection load='5vlq' size='340' side='right'caption='[[5vlq]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5vlq]] is a 2 chain structure. 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 [http://proteopedia.org/fgij/fg.htm?mol=5VLQ FirstGlance]. <br>
+
<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='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>
+
</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>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5vlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vlq OCA], [http://pdbe.org/5vlq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vlq RCSB], [http://www.ebi.ac.uk/pdbsum/5vlq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vlq ProSAT]</span></td></tr>
+
<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>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[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>
-
Glycylation and glutamylation, the posttranslational addition of glycines and glutamates to genetically encoded glutamates in the intrinsically disordered tubulin C-terminal tails, are crucial for the biogenesis and stability of cilia and flagella and play important roles in metazoan development. Members of the diverse family of tubulin tyrosine ligase-like (TTLL) enzymes catalyze these modifications, which are part of an evolutionarily conserved and complex tubulin code that regulates microtubule interactions with cellular effectors. The site specificity of TTLL enzymes and their biochemical interplay remain largely unknown. Here, we report an in vitro characterization of a tubulin glycylase. We show that TTLL3 glycylates the beta-tubulin tail at four sites in a hierarchical order and that TTLL3 and the glutamylase TTLL7 compete for overlapping sites on the tubulin tail, providing a molecular basis for the anticorrelation between glutamylation and glycylation observed in axonemes. This anticorrelation demonstrates how a combinatorial tubulin code written in two different posttranslational modifications can arise through the activities of related but distinct TTLL enzymes. To elucidate what structural elements differentiate TTLL glycylases from glutamylases, with which they share the common TTL scaffold, we determined the TTLL3 X-ray structure at 2.3-A resolution. This structure reveals two architectural elements unique to glycyl initiases and critical for their activity. Thus, our work sheds light on the structural and functional diversification of TTLL enzymes, and constitutes an initial important step toward understanding how the tubulin code is written through the intersection of activities of multiple TTLL enzymes.
+
-
 
+
-
Crystal structure of tubulin tyrosine ligase-like 3 reveals essential architectural elements unique to tubulin monoglycylases.,Garnham CP, Yu I, Li Y, Roll-Mecak A 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<ref>PMID:28576883</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5vlq" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>
Line 21: Line 15:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Garnham, C P]]
+
[[Category: Xenopus tropicalis]]
-
[[Category: Li, Y]]
+
[[Category: Garnham CP]]
-
[[Category: Roll-Mecak, A]]
+
[[Category: Li Y]]
-
[[Category: Yu, I]]
+
[[Category: Roll-Mecak A]]
-
[[Category: Glycylase]]
+
[[Category: Yu I]]
-
[[Category: Ligase]]
+
-
[[Category: Microtubule]]
+
-
[[Category: Ttll3]]
+
-
[[Category: Tubulin]]
+

Current revision

Structure of the TTLL3 Glycylase

PDB ID 5vlq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5vlq"
Personal tools