1y64
From Proteopedia
(New page: 200px<br /><applet load="1y64" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y64, resolution 3.05Å" /> '''Bni1p Formin Homolog...) |
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| - | [[Image:1y64.gif|left|200px]]<br /><applet load="1y64" size=" | + | [[Image:1y64.gif|left|200px]]<br /><applet load="1y64" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1y64, resolution 3.05Å" /> | caption="1y64, resolution 3.05Å" /> | ||
'''Bni1p Formin Homology 2 Domain complexed with ATP-actin'''<br /> | '''Bni1p Formin Homology 2 Domain complexed with ATP-actin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The conserved formin homology 2 (FH2) domain nucleates actin filaments and | + | The conserved formin homology 2 (FH2) domain nucleates actin filaments and remains bound to the barbed end of the growing filament. Here we report the crystal structure of the yeast Bni1p FH2 domain in complex with tetramethylrhodamine-actin. Each of the two structural units in the FH2 dimer binds two actins in an orientation similar to that in an actin filament, suggesting that this structure could function as a filament nucleus. Biochemical properties of heterodimeric FH2 mutants suggest that the wild-type protein equilibrates between two bound states at the barbed end: one permitting monomer binding and the other permitting monomer dissociation. Interconversion between these states allows processive barbed-end polymerization and depolymerization in the presence of bound FH2 domain. Kinetic and/or thermodynamic differences in the conformational and binding equilibria can explain the variable activity of different FH2 domains as well as the effects of the actin-binding protein profilin on FH2 function. |
==About this Structure== | ==About this Structure== | ||
| - | 1Y64 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with CA and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1Y64 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y64 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Otomo, C.]] | [[Category: Otomo, C.]] | ||
[[Category: Otomo, T.]] | [[Category: Otomo, T.]] | ||
| - | [[Category: Panchal, S | + | [[Category: Panchal, S C.]] |
| - | [[Category: Rosen, M | + | [[Category: Rosen, M K.]] |
| - | [[Category: Tomchick, D | + | [[Category: Tomchick, D R.]] |
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: tetramethylrhodamine-5-maleimide]] | [[Category: tetramethylrhodamine-5-maleimide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:02:05 2008'' |
Revision as of 14:02, 21 February 2008
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Bni1p Formin Homology 2 Domain complexed with ATP-actin
Overview
The conserved formin homology 2 (FH2) domain nucleates actin filaments and remains bound to the barbed end of the growing filament. Here we report the crystal structure of the yeast Bni1p FH2 domain in complex with tetramethylrhodamine-actin. Each of the two structural units in the FH2 dimer binds two actins in an orientation similar to that in an actin filament, suggesting that this structure could function as a filament nucleus. Biochemical properties of heterodimeric FH2 mutants suggest that the wild-type protein equilibrates between two bound states at the barbed end: one permitting monomer binding and the other permitting monomer dissociation. Interconversion between these states allows processive barbed-end polymerization and depolymerization in the presence of bound FH2 domain. Kinetic and/or thermodynamic differences in the conformational and binding equilibria can explain the variable activity of different FH2 domains as well as the effects of the actin-binding protein profilin on FH2 function.
About this Structure
1Y64 is a Protein complex structure of sequences from Oryctolagus cuniculus and Saccharomyces cerevisiae with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain., Otomo T, Tomchick DR, Otomo C, Panchal SC, Machius M, Rosen MK, Nature. 2005 Feb 3;433(7025):488-94. Epub 2005 Jan 5. PMID:15635372
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