1z5w
From Proteopedia
(New page: 200px<br /> <applet load="1z5w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z5w, resolution 3.00Å" /> '''Crystal Structure o...) |
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| - | [[Image:1z5w.gif|left|200px]]<br /> | + | [[Image:1z5w.gif|left|200px]]<br /><applet load="1z5w" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1z5w" size=" | + | |
caption="1z5w, resolution 3.00Å" /> | caption="1z5w, resolution 3.00Å" /> | ||
'''Crystal Structure of gamma-tubulin bound to GTP'''<br /> | '''Crystal Structure of gamma-tubulin bound to GTP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Microtubules are hollow polymers of alphabeta-tubulin that show | + | Microtubules are hollow polymers of alphabeta-tubulin that show GTP-dependent assembly dynamics and comprise a critical part of the eukaryotic cytoskeleton. Initiation of new microtubules in vivo requires gamma-tubulin, organized as an oligomer within the 2.2-MDa gamma-tubulin ring complex (gamma-TuRC) of higher eukaryotes. Structural insight is lacking regarding gamma-tubulin, its oligomerization and how it promotes microtubule assembly. Here we report the 2.7-A crystal structure of human gamma-tubulin bound to GTP-gammaS (a non-hydrolysable GTP analogue). We observe a 'curved' conformation for gamma-tubulin-GTPgammaS, similar to that seen for GDP-bound, unpolymerized alphabeta-tubulin. Tubulins are thought to represent a distinct class of GTP-binding proteins, and conformational switching in gamma-tubulin might differ from the nucleotide-dependent switching of signalling GTPases. A crystal packing interaction replicates the lateral contacts between alpha- and beta-tubulins in the microtubule, and this association probably forms the basis for gamma-tubulin oligomerization within the gamma-TuRC. Laterally associated gamma-tubulins in the gamma-TuRC might promote microtubule nucleation by providing a template that enhances the intrinsically weak lateral interaction between alphabeta-tubulin heterodimers. Because they are dimeric, alphabeta-tubulins cannot form microtubule-like lateral associations in the curved conformation. The lateral array of gamma-tubulins we observe in the crystal reveals a unique functional property of a monomeric tubulin. |
==About this Structure== | ==About this Structure== | ||
| - | 1Z5W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and GTP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1Z5W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GTP:'>GTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z5W OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Agard, D | + | [[Category: Agard, D A.]] |
| - | [[Category: Aldaz, H | + | [[Category: Aldaz, H A.]] |
| - | [[Category: Rice, L | + | [[Category: Rice, L M.]] |
[[Category: Stearns, T.]] | [[Category: Stearns, T.]] | ||
[[Category: GTP]] | [[Category: GTP]] | ||
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[[Category: complex with gtp]] | [[Category: complex with gtp]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:22 2008'' |
Revision as of 14:12, 21 February 2008
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Crystal Structure of gamma-tubulin bound to GTP
Overview
Microtubules are hollow polymers of alphabeta-tubulin that show GTP-dependent assembly dynamics and comprise a critical part of the eukaryotic cytoskeleton. Initiation of new microtubules in vivo requires gamma-tubulin, organized as an oligomer within the 2.2-MDa gamma-tubulin ring complex (gamma-TuRC) of higher eukaryotes. Structural insight is lacking regarding gamma-tubulin, its oligomerization and how it promotes microtubule assembly. Here we report the 2.7-A crystal structure of human gamma-tubulin bound to GTP-gammaS (a non-hydrolysable GTP analogue). We observe a 'curved' conformation for gamma-tubulin-GTPgammaS, similar to that seen for GDP-bound, unpolymerized alphabeta-tubulin. Tubulins are thought to represent a distinct class of GTP-binding proteins, and conformational switching in gamma-tubulin might differ from the nucleotide-dependent switching of signalling GTPases. A crystal packing interaction replicates the lateral contacts between alpha- and beta-tubulins in the microtubule, and this association probably forms the basis for gamma-tubulin oligomerization within the gamma-TuRC. Laterally associated gamma-tubulins in the gamma-TuRC might promote microtubule nucleation by providing a template that enhances the intrinsically weak lateral interaction between alphabeta-tubulin heterodimers. Because they are dimeric, alphabeta-tubulins cannot form microtubule-like lateral associations in the curved conformation. The lateral array of gamma-tubulins we observe in the crystal reveals a unique functional property of a monomeric tubulin.
About this Structure
1Z5W is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Insights into microtubule nucleation from the crystal structure of human gamma-tubulin., Aldaz H, Rice LM, Stearns T, Agard DA, Nature. 2005 May 26;435(7041):523-7. PMID:15917813
Page seeded by OCA on Thu Feb 21 16:12:22 2008
Categories: Homo sapiens | Single protein | Agard, D A. | Aldaz, H A. | Rice, L M. | Stearns, T. | GTP | MG | Complex with gtp
