5BVR
Actin binding domain of alpha-actinin from Schizosaccharomyces pombe
Summary for 5BVR
| Entry DOI | 10.2210/pdb5bvr/pdb |
| Descriptor | Alpha-actinin-like protein 1, ZINC ION (3 entities in total) |
| Functional Keywords | alpha-actinin actin binding schizosaccharomyces pombe, cell division, cell cycle |
| Biological source | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Cellular location | Cytoplasm, cytoskeleton : O13728 |
| Total number of polymer chains | 1 |
| Total formula weight | 27488.47 |
| Authors | Persson, K.,Backman, L.,Addario, B. (deposition date: 2015-06-05, release date: 2016-03-23, Last modification date: 2024-01-10) |
| Primary citation | Addario, B.,Sandblad, L.,Persson, K.,Backman, L. Characterisation of Schizosaccharomyces pombe alpha-actinin. Peerj, 4:e1858-e1858, 2016 Cited by PubMed Abstract: The actin cytoskeleton plays a fundamental role in eukaryotic cells. Its reorganization is regulated by a plethora of actin-modulating proteins, such as a-actinin. In higher organisms, α-actinin is characterized by the presence of three distinct structural domains: an N-terminal actin-binding domain and a C-terminal region with EF-hand motif separated by a central rod domain with four spectrin repeats. Sequence analysis has revealed that the central rod domain of α-actinin from the fission yeast Schizosaccharomyces pombe consists of only two spectrin repeats. To obtain a firmer understanding of the structure and function of this unconventional α-actinin, we have cloned and characterized each structural domain. Our results show that this a-actinin isoform is capable of forming dimers and that the rod domain is required for this. However, its actin-binding and cross-linking activity appears less efficient compared to conventional α-actinins. The solved crystal structure of the actin-binding domain indicates that the closed state is stabilised by hydrogen bonds and a salt bridge not present in other α-actinins, which may reduce the affinity for actin. PubMed: 27069798DOI: 10.7717/peerj.1858 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.46 Å) |
Structure validation
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