3j7i

<StructureSection load='3j7i' size='340' side='right' caption='[[3j7i]], [[Resolution|resolution]] 8.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[3j7i]] is a 2 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=3J7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J7I FirstGlance]. <br>

</td></tr><tr id='ligand'><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></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=3j7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j7i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j7i RCSB], [http://www.ebi.ac.uk/pdbsum/3j7i PDBsum]</span></td></tr>

== Publication Abstract from PubMed ==

Microtubules are dynamic polymers that stochastically switch between growing and shrinking phases. Microtubule dynamics are regulated by guanosine triphosphate (GTP) hydrolysis by beta-tubulin, but the mechanism of this regulation remains elusive because high-resolution microtubule structures have only been revealed for the guanosine diphosphate (GDP) state. In this paper, we solved the cryoelectron microscopy (cryo-EM) structure of microtubule stabilized with a GTP analogue, guanylyl 5'-alpha,beta-methylenediphosphonate (GMPCPP), at 8.8-A resolution by developing a novel cryo-EM image reconstruction algorithm. In contrast to the crystal structures of GTP-bound tubulin relatives such as gamma-tubulin and bacterial tubulins, significant changes were detected between GMPCPP and GDP-taxol microtubules at the contacts between tubulins both along the protofilament and between neighboring protofilaments, contributing to the stability of the microtubule. These findings are consistent with the structural plasticity or lattice model and suggest the structural basis not only for the regulatory mechanism of microtubule dynamics but also for the recognition of the nucleotide state of the microtubule by several microtubule-binding proteins, such as EB1 or kinesin.

 

== References ==

</StructureSection>

[[Category: Hirokawa, N]]

[[Category: Nitta, R]]

[[Category: Ogura, T]]

[[Category: Okada, Y]]

[[Category: Sato, C]]

[[Category: Yajima, H]]

[[Category: Tubulin]]