3tin: Difference between revisions
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==Tubulin tyrosine ligase== | ==Tubulin tyrosine ligase== | ||
<StructureSection load='3tin' size='340' side='right' caption='[[3tin]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='3tin' size='340' side='right' caption='[[3tin]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3tin]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3tin]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TIN FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tig|3tig]], [[3tii|3tii]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tig|3tig]], [[3tii|3tii]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ttl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ttl ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tin OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tin RCSB], [http://www.ebi.ac.uk/pdbsum/3tin PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tin OCA], [http://pdbe.org/3tin PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tin RCSB], [http://www.ebi.ac.uk/pdbsum/3tin PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tin ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3tin" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Tubulin tyrosine ligase|Tubulin tyrosine ligase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Deaconescu, A]] | [[Category: Deaconescu, A]] | ||
[[Category: Piszczek, G]] | [[Category: Piszczek, G]] | ||
Revision as of 10:28, 11 August 2016
Tubulin tyrosine ligaseTubulin tyrosine ligase
Structural highlights
Publication Abstract from PubMedTubulin 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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