3tin: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:3tin.png|left|200px]]
+==Tubulin tyrosine ligase==
+<StructureSection load='3tin' size='340' side='right' caption='[[3tin]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3tin]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota]. 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><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><br>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tig|3tig]], [[3tii|3tii]]</td></tr>
+<tr><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=2759 Eukaryota])</td></tr>
+<tr><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>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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>
-The line below this paragraph, containing "STRUCTURE_3tin", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_3tin|  PDB=3tin  |  SCENE=  }}
-===Tubulin tyrosine ligase===
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
-<!--
+<references/>
-The line below this paragraph, {{ABSTRACT_PUBMED_22020298}}, adds the Publication Abstract to the page
+__TOC__
-(as it appears on PubMed at http://www.pubmed.gov), where 22020298 is the PubMed ID number.
+</StructureSection>
--->
-{{ABSTRACT_PUBMED_22020298}}
-==About this Structure==
-[[3tin]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TIN OCA].
-==Reference==
-<ref group="xtra">PMID:022020298</ref><references group="xtra"/>
 [[Category: Eukaryota]]
 [[Category: Deaconescu, A.]]