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| - | [[Image:1z5w.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1z5w| PDB=1z5w | SCENE= }} | | {{STRUCTURE_1z5w| PDB=1z5w | SCENE= }} |
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| - | '''Crystal Structure of gamma-tubulin bound to GTP'''
| + | ===Crystal Structure of gamma-tubulin bound to GTP=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15917813}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15917813 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15917813}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Stearns, T.]] | | [[Category: Stearns, T.]] |
| | [[Category: Complex with gtp]] | | [[Category: Complex with gtp]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:12:32 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:44:24 2008'' |
Revision as of 06:44, 29 July 2008
Template:STRUCTURE 1z5w
Crystal Structure of gamma-tubulin bound to GTP
Template:ABSTRACT PUBMED 15917813
About this Structure
1Z5W is a Single protein structure of sequence from Homo sapiens. 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 Tue Jul 29 09:44:24 2008
