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2ff3
From Proteopedia
| 2ff3, resolution 2.00Å () | |||||||||
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| Ligands: | , | ||||||||
| Domains: | GEL, ACTIN, Actin | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin
Participation of actin in cellular processes relies on the dynamics of filament assembly. Filament elongation is fed by monomeric actin in complex with either profilin or a Wiscott-Aldrich syndrome protein (WASP) homology domain 2 (WH2)/beta-thymosin (betaT) domain. WH2/betaT motif repetition (typified by ciboulot) or combination with nonrelated domains (as found in N-WASP) results in proteins that yield their actin to filament elongation. Here, we report the crystal structures of actin bound hybrid proteins, constructed between gelsolin and WH2/betaT domains from ciboulot or N-WASP. We observe the C-terminal half of ciboulot domain 2 bound to actin. In solution, we show that cibolout domains 2 and 3 bind to both G- and F-actin, and that whole ciboulot forms a complex with two actin monomers. In contrast, the analogous portion of N-WASP WH2 domain 2 is detached from actin, indicating that the C-terminal halves of the betaT and WH2 motifs are not functionally analogous.
The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins., Aguda AH, Xue B, Irobi E, Preat T, Robinson RC, Structure. 2006 Mar;14(3):469-76. PMID:16531231
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2FF3 is a 3 chains structure of sequences from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
- Aguda AH, Xue B, Irobi E, Preat T, Robinson RC. The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins. Structure. 2006 Mar;14(3):469-76. PMID:16531231 doi:10.1016/j.str.2005.12.011
Page seeded by OCA on Tue Feb 17 03:55:08 2009
