3ZID
CetZ from Methanosaeta thermophila strain DSM 6194
3ZID の概要
| エントリーDOI | 10.2210/pdb3zid/pdb |
| 分子名称 | TUBULIN/FTSZ, GTPASE, GUANOSINE-5'-DIPHOSPHATE (3 entities in total) |
| 機能のキーワード | gtp-binding protein, tubz, phuz, cytoskeleton |
| 由来する生物種 | METHANOSAETA THERMOPHILA |
| 細胞内の位置 | Cytoplasm : A0B5R2 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 85166.99 |
| 構造登録者 | |
| 主引用文献 | Duggin, I.G.,Aylett, C.H.S.,Walsh, J.C.,Michie, K.A.,Wang, Q.,Turnbull, L.,Dawson, E.M.,Harry, E.J.,Whitchurch, C.B.,Amos, A.,Lowe, J. Cetz Tubulin-Like Proteins Control Archaeal Cell Shape Nature, 519:362-, 2015 Cited by PubMed Abstract: Tubulin is a major component of the eukaryotic cytoskeleton, controlling cell shape, structure and dynamics, whereas its bacterial homologue FtsZ establishes the cytokinetic ring that constricts during cell division. How such different roles of tubulin and FtsZ evolved is unknown. Studying Archaea may provide clues as these organisms share characteristics with Eukarya and Bacteria. Here we report the structure and function of proteins from a distinct family related to tubulin and FtsZ, named CetZ, which co-exists with FtsZ in many archaea. CetZ X-ray crystal structures showed the FtsZ/tubulin superfamily fold, and one crystal form contained sheets of protofilaments, suggesting a structural role. However, inactivation of CetZ proteins in Haloferax volcanii did not affect cell division. Instead, CetZ1 was required for differentiation of the irregular plate-shaped cells into a rod-shaped cell type that was essential for normal swimming motility. CetZ1 formed dynamic cytoskeletal structures in vivo, relating to its capacity to remodel the cell envelope and direct rod formation. CetZ2 was also implicated in H. volcanii cell shape control. Our findings expand the known roles of the FtsZ/tubulin superfamily to include archaeal cell shape dynamics, suggesting that a cytoskeletal role might predate eukaryotic cell evolution, and they support the premise that a major function of the microbial rod shape is to facilitate swimming. PubMed: 25533961DOI: 10.1038/NATURE13983 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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