1nr0

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[[Image:1nr0.gif|left|200px]]<br /><applet load="1nr0" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nr0.gif|left|200px]]
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caption="1nr0, resolution 1.70&Aring;" />
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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).'''<br />
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{{Structure
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|PDB= 1nr0 |SIZE=350|CAPTION= <scene name='initialview01'>1nr0</scene>, resolution 1.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene>
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|ACTIVITY=
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|GENE= UNC-78 OR C04F6.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans])
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}}
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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).'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1NR0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NR0 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15150269 15150269]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15150269 15150269]
[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: protein structure initiative]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: psi]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
[[Category: wd40 repeat]]
[[Category: wd40 repeat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:00:32 2008''

Revision as of 11:00, 20 March 2008

Image:1nr0.gif


PDB ID 1nr0

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands:
Gene: UNC-78 OR C04F6.4 (Caenorhabditis elegans)
Coordinates: save as pdb, mmCIF, xml



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. 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 Mar 20 13:00:32 2008

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