2Q36
Actin Dimer Cross-linked between Residues 191 and 374 and complexed with Kabiramide C
Summary for 2Q36
| Entry DOI | 10.2210/pdb2q36/pdb |
| Related | 1QZ5 2Q31 |
| Descriptor | Actin, alpha skeletal muscle, CALCIUM ION, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | cross-linked dimer, structural protein |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Cellular location | Cytoplasm, cytoskeleton: P68135 |
| Total number of polymer chains | 1 |
| Total formula weight | 43548.13 |
| Authors | Sawaya, M.R.,Pashkov, I.,Kudryashov, D.S.,Reisler, E.,Yeates, T.O. (deposition date: 2007-05-29, release date: 2007-06-05, Last modification date: 2023-08-30) |
| Primary citation | Sawaya, M.R.,Kudryashov, D.S.,Pashkov, I.,Adisetiyo, H.,Reisler, E.,Yeates, T.O. Multiple crystal structures of actin dimers and their implications for interactions in the actin filament. Acta Crystallogr.,Sect.D, 64:454-465, 2008 Cited by PubMed Abstract: The structure of actin in its monomeric form is known at high resolution, while the structure of filamentous F-actin is only understood at considerably lower resolution. Knowing precisely how the monomers of actin fit together would lead to a deeper understanding of the dynamic behavior of the actin filament. Here, a series of crystal structures of actin dimers are reported which were prepared by cross-linking in either the longitudinal or the lateral direction in the filament state. Laterally cross-linked dimers, comprised of monomers belonging to different protofilaments, are found to adopt configurations in crystals that are not related to the native structure of filamentous actin. In contrast, multiple structures of longitudinal dimers consistently reveal the same interface between monomers within a single protofilament. The reappearance of the same longitudinal interface in multiple crystal structures adds weight to arguments that the interface visualized is similar to that in actin filaments. Highly conserved atomic interactions involving residues 199-205 and 287-291 are highlighted. PubMed: 18391412DOI: 10.1107/S0907444908003351 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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