4u3j
From Proteopedia
(Difference between revisions)
m (Protected "4u3j" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | ''' | + | ==TOG2:alpha/beta-tubulin complex== |
| + | <StructureSection load='4u3j' size='340' side='right' caption='[[4u3j]], [[Resolution|resolution]] 2.81Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4u3j]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U3J FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br> | ||
| + | <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=4u3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u3j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u3j RCSB], [http://www.ebi.ac.uk/pdbsum/4u3j PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Stu2p/XMAP215 proteins are essential microtubule polymerases that use multiple alphabeta-tubulin-interacting TOG domains to bind microtubule plus ends and catalyze fast microtubule growth. We report here the structure of the TOG2 domain from Stu2p bound to yeast alphabeta-tubulin. Like TOG1, TOG2 binds selectively to a fully 'curved' conformation of alphabeta-tubulin, incompatible with a microtubule lattice. We also show that TOG1-TOG2 binds non-cooperatively to two alphabeta-tubulins. Preferential interactions between TOGs and fully curved alphabeta-tubulin that cannot exist elsewhere in the microtubule explain how these polymerases localize to the extreme microtubule end. We propose that these polymerases promote elongation because their linked TOG domains concentrate unpolymerized alphabeta-tubulin near curved subunits already bound at the microtubule end. This tethering model can explain catalyst-like behavior and also predicts that the polymerase action changes the configuration of the microtubule end. | ||
| - | + | A tethered delivery mechanism explains the catalytic action of a microtubule polymerase.,Ayaz P, Munyoki S, Geyer EA, Piedra FA, Vu ES, Bromberg R, Otwinowski Z, Grishin NV, Brautigam CA, Rice LM Elife. 2014 Aug 5:e03069. doi: 10.7554/eLife.03069. PMID:25097237<ref>PMID:25097237</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Ayaz, P.]] | ||
| + | [[Category: Rice, L M.]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Structural protein-protein binding complex]] | ||
Revision as of 16:16, 20 August 2014
TOG2:alpha/beta-tubulin complex
| |||||||||||
