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1nr0
From Proteopedia
(New page: 200px<br /><applet load="1nr0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nr0, resolution 1.70Å" /> '''Two Seven-Bladed Bet...) |
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| - | [[Image:1nr0.gif|left|200px]]<br /><applet load="1nr0" size=" | + | [[Image:1nr0.gif|left|200px]]<br /><applet load="1nr0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nr0, resolution 1.70Å" /> | caption="1nr0, resolution 1.70Å" /> | ||
'''Two Seven-Bladed Beta-Propeller Domains Revealed By The Structure Of A C. elegans Homologue Of Yeast Actin Interacting Protein 1 (AIP1).'''<br /> | '''Two Seven-Bladed Beta-Propeller Domains Revealed By The Structure Of A C. elegans Homologue Of Yeast Actin Interacting Protein 1 (AIP1).'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Actin-interacting protein 1 (AIP1) is a WD40 repeat protein that enhances | + | Actin-interacting protein 1 (AIP1) is a WD40 repeat protein that enhances actin filament disassembly in the presence of actin-depolymerizing factor (ADF)/cofilin. AIP1 also caps the barbed end of ADF/cofilin-bound actin filament. However, the mechanism by which AIP1 interacts with ADF/cofilin and actin is not clearly understood. We determined the crystal structure of Caenorhabditis elegans AIP1 (UNC-78), which revealed 14 WD40 modules arranged in two seven-bladed beta-propeller domains. The structure allowed for the mapping of conserved surface residues, and mutagenesis studies identified five residues that affected the ADF/cofilin-dependent actin filament disassembly activity. Mutations of these residues, which reside in blades 3 and 4 in the N-terminal propeller domain, had significant effects on the disassembly activity but did not alter the barbed end capping activity. These data support a model in which this conserved surface of AIP1 plays a direct role in enhancing fragmentation/depolymerization of ADF/cofilin-bound actin filaments but not in barbed end capping. |
==About this Structure== | ==About this Structure== | ||
| - | 1NR0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1NR0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NR0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Almo, S | + | [[Category: Almo, S C.]] |
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
[[Category: Mohri, K.]] | [[Category: Mohri, K.]] | ||
| - | [[Category: NYSGXRC, New | + | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] |
[[Category: Ono, S.]] | [[Category: Ono, S.]] | ||
| - | [[Category: Vorobiev, S | + | [[Category: Vorobiev, S M.]] |
[[Category: MN]] | [[Category: MN]] | ||
[[Category: actin interacting protein]] | [[Category: actin interacting protein]] | ||
| Line 31: | Line 31: | ||
[[Category: wd40 repeat]] | [[Category: wd40 repeat]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:05 2008'' |
Revision as of 12:09, 21 February 2008
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Two Seven-Bladed Beta-Propeller Domains Revealed By The Structure Of A C. elegans Homologue Of Yeast Actin Interacting Protein 1 (AIP1).
Overview
Actin-interacting protein 1 (AIP1) is a WD40 repeat protein that enhances actin filament disassembly in the presence of actin-depolymerizing factor (ADF)/cofilin. AIP1 also caps the barbed end of ADF/cofilin-bound actin filament. However, the mechanism by which AIP1 interacts with ADF/cofilin and actin is not clearly understood. We determined the crystal structure of Caenorhabditis elegans AIP1 (UNC-78), which revealed 14 WD40 modules arranged in two seven-bladed beta-propeller domains. The structure allowed for the mapping of conserved surface residues, and mutagenesis studies identified five residues that affected the ADF/cofilin-dependent actin filament disassembly activity. Mutations of these residues, which reside in blades 3 and 4 in the N-terminal propeller domain, had significant effects on the disassembly activity but did not alter the barbed end capping activity. These data support a model in which this conserved surface of AIP1 plays a direct role in enhancing fragmentation/depolymerization of ADF/cofilin-bound actin filaments but not in barbed end capping.
About this Structure
1NR0 is a Single protein structure of sequence from Caenorhabditis elegans with as ligand. Full crystallographic information is available from OCA.
Reference
Identification of functional residues on Caenorhabditis elegans actin-interacting protein 1 (UNC-78) for disassembly of actin depolymerizing factor/cofilin-bound actin filaments., Mohri K, Vorobiev S, Fedorov AA, Almo SC, Ono S, J Biol Chem. 2004 Jul 23;279(30):31697-707. Epub 2004 May 18. PMID:15150269
Page seeded by OCA on Thu Feb 21 14:09:05 2008
Categories: Caenorhabditis elegans | Single protein | Almo, S C. | Burley, S K. | Mohri, K. | NYSGXRC, New York Structural GenomiX Research Consortium. | Ono, S. | Vorobiev, S M. | MN | Actin interacting protein | Adf | Beta propeller | Cofilin | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomics | Wd40 repeat
