1io0: Difference between revisions
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|PDB= 1io0 |SIZE=350|CAPTION= <scene name='initialview01'>1io0</scene>, resolution 1.45Å | |PDB= 1io0 |SIZE=350|CAPTION= <scene name='initialview01'>1io0</scene>, resolution 1.45Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1io0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io0 OCA], [http://www.ebi.ac.uk/pdbsum/1io0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1io0 RCSB]</span> | |||
}} | }} | ||
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[[Category: Maeda, Y.]] | [[Category: Maeda, Y.]] | ||
[[Category: Yamashita, A.]] | [[Category: Yamashita, A.]] | ||
[[Category: lrr protein]] | [[Category: lrr protein]] | ||
[[Category: right-handed super-helix]] | [[Category: right-handed super-helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:22:18 2008'' | ||
Revision as of 21:22, 30 March 2008
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| , resolution 1.45Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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