4ihj: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of tubulin-stathmin-TTL-ADP complex== | ==Crystal structure of tubulin-stathmin-TTL-ADP complex== | ||
<StructureSection load='4ihj' size='340' side='right' caption='[[4ihj]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4ihj' size='340' side='right'caption='[[4ihj]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ihj]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ihj]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IHJ 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | </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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4ihj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ihj OCA], [https://pdbe.org/4ihj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ihj RCSB], [https://www.ebi.ac.uk/pdbsum/4ihj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ihj ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/TBA1B_BOVIN TBA1B_BOVIN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 4ihj" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4ihj" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Stathmin-4 3D structures|Stathmin-4 3D structures]] | |||
*[[Tubulin 3D Structures|Tubulin 3D Structures]] | |||
*[[Tubulin tyrosine ligase|Tubulin tyrosine ligase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 25: | Line 28: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Bargsten | [[Category: Rattus norvegicus]] | ||
[[Category: Frey | [[Category: Bargsten K]] | ||
[[Category: Hoogenraad | [[Category: Frey D]] | ||
[[Category: Janke | [[Category: Hoogenraad CC]] | ||
[[Category: Jaussi | [[Category: Janke C]] | ||
[[Category: Kammerer | [[Category: Jaussi R]] | ||
[[Category: Kuijpers | [[Category: Kammerer RA]] | ||
[[Category: Magiera | [[Category: Kuijpers M]] | ||
[[Category: Prota | [[Category: Magiera MM]] | ||
[[Category: Steinmetz | [[Category: Prota AE]] | ||
[[Category: Wieser | [[Category: Steinmetz MO]] | ||
[[Category: Wieser M]] | |||
Revision as of 23:45, 16 November 2022
Crystal structure of tubulin-stathmin-TTL-ADP complexCrystal structure of tubulin-stathmin-TTL-ADP complex
Structural highlights
FunctionTBA1B_BOVIN Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. Publication Abstract from PubMedTubulin tyrosine ligase (TTL) catalyzes the post-translational retyrosination of detyrosinated alpha-tubulin. Despite the indispensable role of TTL in cell and organism development, its molecular mechanism of action is poorly understood. By solving crystal structures of TTL in complex with tubulin, we here demonstrate that TTL binds to the alpha and beta subunits of tubulin and recognizes the curved conformation of the dimer. Biochemical and cellular assays revealed that specific tubulin dimer recognition controls the activity of the enzyme, and as a consequence, neuronal development. The TTL-tubulin structure further illustrates how the enzyme binds the functionally crucial C-terminal tail sequence of alpha-tubulin and how this interaction catalyzes the tyrosination reaction. It also reveals how TTL discriminates between alpha- and beta-tubulin, and between different post-translationally modified forms of alpha-tubulin. Together, our data suggest that TTL has specifically evolved to recognize and modify tubulin, thus highlighting a fundamental role of the evolutionary conserved tubulin tyrosination cycle in regulating the microtubule cytoskeleton. Structural basis of tubulin tyrosination by tubulin tyrosine ligase.,Prota AE, Magiera MM, Kuijpers M, Bargsten K, Frey D, Wieser M, Jaussi R, Hoogenraad CC, Kammerer RA, Janke C, Steinmetz MO J Cell Biol. 2013 Feb 4;200(3):259-70. doi: 10.1083/jcb.201211017. Epub 2013 Jan , 28. PMID:23358242[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||