2a5x
From Proteopedia
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Crystal Structure of a Cross-linked Actin Dimer
Overview
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 Structure
2A5X is a Single protein structure of sequence from Oryctolagus cuniculus with , , , and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 16:23:54 2008
Categories: Oryctolagus cuniculus | Single protein | Adisetiyo, H. | Hegyi, G. | Kudryashov, D S. | Norcross, T. | Reisler, E. | Sawaya, M R. | Yeates, T O. | ANP | CA | LAR | MPD | NSB | Muscle protein | Nucleotide-binding | Structural protein
