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4JHD

Crystal Structure of an Actin Dimer in Complex with the Actin Nucleator Cordon-Bleu

Summary for 4JHD
Entry DOI10.2210/pdb4jhd/pdb
DescriptorActin-5C, Protein cordon-bleu, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (6 entities in total)
Functional Keywordsactin cytoskeleton, actin filament nucleator, nuclear actin, nucleation, tandem w domains, structural protein-protein binding complex, structural protein/protein binding
Biological sourceDrosophila melanogaster (Fruit fly)
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Total number of polymer chains6
Total formula weight210235.05
Authors
Chen, X.,Ni, F.,Wang, Q. (deposition date: 2013-03-04, release date: 2013-06-19, Last modification date: 2024-02-28)
Primary citationChen, X.,Ni, F.,Tian, X.,Kondrashkina, E.,Wang, Q.,Ma, J.
Structural basis of actin filament nucleation by tandem w domains.
Cell Rep, 3:1910-1920, 2013
Cited by
PubMed Abstract: Spontaneous nucleation of actin is very inefficient in cells. To overcome this barrier, cells have evolved a set of actin filament nucleators to promote rapid nucleation and polymerization in response to specific stimuli. However, the molecular mechanism of actin nucleation remains poorly understood. This is hindered largely by the fact that actin nucleus, once formed, rapidly polymerizes into filament, thus making it impossible to capture stable multisubunit actin nucleus. Here, we report an effective double-mutant strategy to stabilize actin nucleus by preventing further polymerization. Employing this strategy, we solved the crystal structure of AMPPNP-actin in complex with the first two tandem W domains of Cordon-bleu (Cobl), a potent actin filament nucleator. Further sequence comparison and functional studies suggest that the nucleation mechanism of Cobl is probably shared by the p53 cofactor JMY, but not Spire. Moreover, the double-mutant strategy opens the way for atomic mechanistic study of actin nucleation and polymerization.
PubMed: 23727244
DOI: 10.1016/j.celrep.2013.04.028
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.91 Å)
Structure validation

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