2A5X
Crystal Structure of a Cross-linked Actin Dimer
Summary for 2A5X
| Entry DOI | 10.2210/pdb2a5x/pdb |
| Descriptor | Actin, alpha skeletal muscle, CALCIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (7 entities in total) |
| Functional Keywords | muscle protein, nucleotide-binding, structural protein, contractile protein |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Cellular location | Cytoplasm, cytoskeleton: P68135 |
| Total number of polymer chains | 1 |
| Total formula weight | 43289.12 |
| Authors | Kudryashov, D.S.,Sawaya, M.R.,Adisetiyo, H.,Norcross, T.,Hegyi, G.,Reisler, E.,Yeates, T.O. (deposition date: 2005-07-01, release date: 2005-08-23, Last modification date: 2023-08-23) |
| Primary citation | Kudryashov, D.S.,Sawaya, M.R.,Adisetiyo, H.,Norcross, T.,Hegyi, G.,Reisler, E.,Yeates, T.O. The crystal structure of a cross-linked actin dimer suggests a detailed molecular interface in F-actin Proc.Natl.Acad.Sci.Usa, 102:13105-13110, 2005 Cited by PubMed Abstract: 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. PubMed: 16141336DOI: 10.1073/pnas.0506429102 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.49 Å) |
Structure validation
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