1io0: Difference between revisions
New page: left|200px<br /><applet load="1io0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1io0, resolution 1.45Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1io0.gif|left|200px]]<br /><applet load="1io0" size=" | [[Image:1io0.gif|left|200px]]<br /><applet load="1io0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1io0, resolution 1.45Å" /> | caption="1io0, resolution 1.45Å" /> | ||
'''CRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALF'''<br /> | '''CRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALF'''<br /> | ||
==Overview== | ==Overview== | ||
Tropomodulin is the unique pointed-end capping protein of the | 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 Structure== | ==About this Structure== | ||
1IO0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1IO0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO0 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: right-handed super-helix]] | [[Category: right-handed super-helix]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:48 2008'' | ||
Revision as of 14:13, 21 February 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 with as ligand. 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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