2a5x
Crystal Structure of a Cross-linked Actin Dimer
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OverviewOverview
The 2.5-A resolution crystal structure is reported for an actin dimer, composed of two protomers cross-linked along the longitudinal (or, vertical) direction of the F-actin filament. The crystal structure, provides an atomic resolution view of a molecular interface between actin, protomers, which we argue represents a near-native interaction in the, F-actin filament. The interaction involves subdomains 3 and 4 from, distinct protomers. The atomic positions in the interface visualized, differ by 5-10 A from those suggested by previous models of F-actin. Such, differences fall within the range of uncertainties allowed by the fiber, diffraction and electron microscopy methods on which previous models have, been based. In the crystal, the translational arrangement of protomers, lacks the slow twist found in native filaments. A plausible model of, F-actin can be constructed by reintroducing the known filament twist, without disturbing significantly the interface observed in the actin dimer, crystal.
About this StructureAbout this Structure
2A5X is a Single protein structure of sequence from Oryctolagus cuniculus with CA, ANP, LAR, NSB and MPD as ligands. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of a cross-linked actin dimer suggests a detailed molecular interface in F-actin., Kudryashov DS, Sawaya MR, Adisetiyo H, Norcross T, Hegyi G, Reisler E, Yeates TO, Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13105-10. Epub 2005 Sep 1. PMID:16141336
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