1pev: Difference between revisions
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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]) | |GENE= UNC-78 OR C04F6.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans]) | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00200 WD40], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG2319 COG2319]</span> | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pev OCA], [http://www.ebi.ac.uk/pdbsum/1pev PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1pev RCSB]</span> | |||
}} | }} | ||
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[[Category: wd40 repeat]] | [[Category: wd40 repeat]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:00:35 2008'' | ||
Revision as of 07:00, 26 March 2008
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| , resolution 2.00Å | |||||||
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| Gene: | UNC-78 OR C04F6.4 (Caenorhabditis elegans) | ||||||
| Domains: | WD40, COG2319 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Actin Interacting Protein from Caenorhabditis Elegans
OverviewOverview
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 StructureAbout this Structure
1PEV is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.
ReferenceReference
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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Caenorhabditis elegans
- Single protein
- Almo, S C.
- Burley, S K.
- Fedorov, A A.
- Mohri, K.
- NYSGXRC, New York Structural GenomiX Research Consortium.
- Ono, S.
- Vorobiev, S.
- Actin interacting protein
- Adf
- Beta propeller
- Cofilin
- New york structural genomix research consortium
- Nysgxrc
- Protein structure initiative
- Psi
- Structural genomic
- Wd40 repeat