3j6f: Difference between revisions
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''' | ==Minimized average structure of GDP-bound dynamic microtubules== | ||
<StructureSection load='3j6f' size='340' side='right' caption='[[3j6f]], [[Resolution|resolution]] 4.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3j6f]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J6F FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j6e|3j6e]], [[3j6g|3j6g]]</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=3j6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j6f RCSB], [http://www.ebi.ac.uk/pdbsum/3j6f PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Dynamic instability, the stochastic switching between growth and shrinkage, is essential for microtubule function. This behavior is driven by GTP hydrolysis in the microtubule lattice and is inhibited by anticancer agents like Taxol. We provide insight into the mechanism of dynamic instability, based on high-resolution cryo-EM structures (4.7-5.6 A) of dynamic microtubules and microtubules stabilized by GMPCPP or Taxol. We infer that hydrolysis leads to a compaction around the E-site nucleotide at longitudinal interfaces, as well as movement of the alpha-tubulin intermediate domain and H7 helix. Displacement of the C-terminal helices in both alpha- and beta-tubulin subunits suggests an effect on interactions with binding partners that contact this region. Taxol inhibits most of these conformational changes, allosterically inducing a GMPCPP-like state. Lateral interactions are similar in all conditions we examined, suggesting that microtubule lattice stability is primarily modulated at longitudinal interfaces. | |||
High-Resolution Microtubule Structures Reveal the Structural Transitions in alphabeta-Tubulin upon GTP Hydrolysis.,Alushin GM, Lander GC, Kellogg EH, Zhang R, Baker D, Nogales E Cell. 2014 May 22;157(5):1117-29. doi: 10.1016/j.cell.2014.03.053. PMID:24855948<ref>PMID:24855948</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Sus scrofa]] | |||
[[Category: Alushin, G M.]] | |||
[[Category: Baker, D.]] | |||
[[Category: Kellogg, E H.]] | |||
[[Category: Lander, G C.]] | |||
[[Category: Nogales, E.]] | |||
[[Category: Zhang, R.]] | |||
[[Category: Dynamic]] | |||
[[Category: Gdp]] | |||
[[Category: Microtubule]] | |||
[[Category: Structural protein]] | |||
Revision as of 08:07, 4 June 2014
Minimized average structure of GDP-bound dynamic microtubulesMinimized average structure of GDP-bound dynamic microtubules
Structural highlights
Publication Abstract from PubMedDynamic instability, the stochastic switching between growth and shrinkage, is essential for microtubule function. This behavior is driven by GTP hydrolysis in the microtubule lattice and is inhibited by anticancer agents like Taxol. We provide insight into the mechanism of dynamic instability, based on high-resolution cryo-EM structures (4.7-5.6 A) of dynamic microtubules and microtubules stabilized by GMPCPP or Taxol. We infer that hydrolysis leads to a compaction around the E-site nucleotide at longitudinal interfaces, as well as movement of the alpha-tubulin intermediate domain and H7 helix. Displacement of the C-terminal helices in both alpha- and beta-tubulin subunits suggests an effect on interactions with binding partners that contact this region. Taxol inhibits most of these conformational changes, allosterically inducing a GMPCPP-like state. Lateral interactions are similar in all conditions we examined, suggesting that microtubule lattice stability is primarily modulated at longitudinal interfaces. High-Resolution Microtubule Structures Reveal the Structural Transitions in alphabeta-Tubulin upon GTP Hydrolysis.,Alushin GM, Lander GC, Kellogg EH, Zhang R, Baker D, Nogales E Cell. 2014 May 22;157(5):1117-29. doi: 10.1016/j.cell.2014.03.053. PMID:24855948[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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