1io0: Difference between revisions
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[[Image:1io0.gif|left|200px]] | [[Image:1io0.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALF''' | {{Structure | ||
|PDB= 1io0 |SIZE=350|CAPTION= <scene name='initialview01'>1io0</scene>, resolution 1.45Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALF''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1IO0 is a [ | 1IO0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO0 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping., Krieger I, Kostyukova A, Yamashita A, Nitanai Y, Maeda Y, Biophys J. 2002 Nov;83(5):2716-25. PMID:[http:// | Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping., Krieger I, Kostyukova A, Yamashita A, Nitanai Y, Maeda Y, Biophys J. 2002 Nov;83(5):2716-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12414704 12414704] | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: right-handed super-helix]] | [[Category: right-handed super-helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:52:44 2008'' | ||
Revision as of 12:52, 20 March 2008
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CRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALF
OverviewOverview
Tropomodulin is the unique pointed-end capping protein of the actin-tropomyosin filament. By blocking elongation and depolymerization, tropomodulin regulates the architecture and the dynamics of the filament. Here we report the crystal structure at 1.45-A resolution of the C-terminal half of tropomodulin (C20), the actin-binding moiety of tropomodulin. C20 is a leucine-rich repeat domain, and this is the first actin-associated protein with a leucine-rich repeat. Binding assays suggested that C20 also interacts with the N-terminal fragment, M1-M2-M3, of nebulin. Based on the crystal structure, we propose a model for C20 docking to the actin subunit at the pointed end. Although speculative, the model is consistent with the idea that a tropomodulin molecule competes with an actin subunit for a pointed end. The model also suggests that interactions with tropomyosin, actin, and nebulin are all possible sources of influences on the dynamic properties of pointed-end capping by tropomodulin.
About this StructureAbout this Structure
1IO0 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping., Krieger I, Kostyukova A, Yamashita A, Nitanai Y, Maeda Y, Biophys J. 2002 Nov;83(5):2716-25. PMID:12414704
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