3tin: Difference between revisions

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<StructureSection load='3tin' size='340' side='right'caption='[[3tin]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='3tin' size='340' side='right'caption='[[3tin]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3tin]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Silurana_(xenopus)_tropicalis Silurana (xenopus) tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TIN FirstGlance]. <br>
<table><tr><td colspan='2'>[[3tin]] is a 1 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=3TIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TIN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tig|3tig]], [[3tii|3tii]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ttl ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8364 Silurana (Xenopus) tropicalis])</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=3tin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tin OCA], [https://pdbe.org/3tin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tin RCSB], [https://www.ebi.ac.uk/pdbsum/3tin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tin ProSAT]</span></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=3tin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tin OCA], [https://pdbe.org/3tin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tin RCSB], [https://www.ebi.ac.uk/pdbsum/3tin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tin ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/F6Z895_XENTR F6Z895_XENTR]
Tubulin tyrosine ligase (TTL) catalyzes the post-translational C-terminal tyrosination of alpha-tubulin. Tyrosination regulates recruitment of microtubule-interacting proteins. TTL is essential. Its loss causes morphogenic abnormalities and is associated with cancers of poor prognosis. We present the first crystal structure of TTL (from Xenopus tropicalis), defining the structural scaffold upon which the diverse TTL-like family of tubulin-modifying enzymes is built. TTL recognizes tubulin using a bipartite strategy. It engages the tubulin tail through low-affinity, high-specificity interactions, and co-opts what is otherwise a homo-oligomerization interface in structurally related ATP grasp-fold enzymes to form a tight hetero-oligomeric complex with the tubulin body. Small-angle X-ray scattering and functional analyses reveal that TTL forms an elongated complex with the tubulin dimer and prevents its incorporation into microtubules by capping the tubulin longitudinal interface, possibly modulating the partition of tubulin between monomeric and polymeric forms.
 
Tubulin tyrosine ligase structure reveals adaptation of an ancient fold to bind and modify tubulin.,Szyk A, Deaconescu AM, Piszczek G, Roll-Mecak A Nat Struct Mol Biol. 2011 Oct 23;18(11):1250-8. doi: 10.1038/nsmb.2148. PMID:22020298<ref>PMID:22020298</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3tin" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Tubulin tyrosine ligase|Tubulin tyrosine ligase]]
*[[Tubulin tyrosine ligase 3D structures|Tubulin tyrosine ligase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Deaconescu, A]]
[[Category: Xenopus tropicalis]]
[[Category: Piszczek, G]]
[[Category: Deaconescu A]]
[[Category: Roll-Mecak, A]]
[[Category: Piszczek G]]
[[Category: Szyk, A]]
[[Category: Roll-Mecak A]]
[[Category: Atp-grasp]]
[[Category: Szyk A]]
[[Category: Ligase]]
[[Category: Tubulin]]
[[Category: Tyrosination]]

Latest revision as of 13:09, 1 March 2024

Tubulin tyrosine ligaseTubulin tyrosine ligase

Structural highlights

3tin is a 1 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 2.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

F6Z895_XENTR

See Also

3tin, resolution 2.90Å

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OCA