5BVR

Actin binding domain of alpha-actinin from Schizosaccharomyces pombe

5BVR の概要

• エントリーDOI: 10.2210/pdb5bvr/pdb
• 分子名称: Alpha-actinin-like protein 1, ZINC ION (3 entities in total)
• 機能のキーワード: alpha-actinin actin binding schizosaccharomyces pombe, cell division, cell cycle
• 由来する生物種: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
• 細胞内の位置: Cytoplasm, cytoskeleton : O13728
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27488.47

構造登録者

Persson, K.,Backman, L.,Addario, B. (登録日: 2015-06-05, 公開日: 2016-03-23, 最終更新日: 2024-01-10)

主引用文献

Addario, B.,Sandblad, L.,Persson, K.,Backman, L.
Characterisation of Schizosaccharomyces pombe alpha-actinin.
Peerj, 4:e1858-e1858, 2016

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: 27069798
DOI: 10.7717/peerj.1858

実験手法

X-RAY DIFFRACTION (1.46 Å)