5FO3
ZapC cell division regulator from E. coli
5FO3 の概要
| エントリーDOI | 10.2210/pdb5fo3/pdb |
| 分子名称 | CELL DIVISION PROTEIN ZAPC (1 entity in total) |
| 機能のキーワード | cell cycle, ftsz, bacterial cell division, z-ring associated protein c |
| 由来する生物種 | ESCHERICHIA COLI |
| 細胞内の位置 | Cytoplasm : P75862 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 42161.43 |
| 構造登録者 | Ortiz, C.,Kureisaite-Ciziene, D.,Schmitz, F.,Vicente, M.,Lowe, J. (登録日: 2015-11-18, 公開日: 2015-11-25, 最終更新日: 2024-11-06) |
| 主引用文献 | Ortiz, C.,Kureisaite-Ciziene, D.,Schmitz, F.,Mclaughlin, S.H.,Vicente, M.,Lowe, J. Crystal Structure of the Z-Ring Associated Cell Division Protein Zapc from Escherichia Coli. FEBS Lett., 589:3822-, 2015 Cited by PubMed Abstract: Bacterial cell division involves a contractile ring that organises downstream proteins at the division site and which contains the tubulin homologue FtsZ. ZapC has been discovered as a non-essential regulator of FtsZ. It localises to the septal ring and deletion of zapC leads to a mild phenotype, while overexpression inhibits cell division. Interference with cell division is facilitated by an interaction with FtsZ. Here, we present the 2.9 Å crystal structure of ZapC from Escherichia coli. ZapC forms a dimer and comprises two domains that belong to the Royal superfamily of which many members bind methylated arginines or lysines. ZapC contains an N-terminal chromo-like domain and a Tudor-like C-terminal domain. We show by ITC that ZapC binds the C-terminal tail of FtsZ. PubMed: 26619764DOI: 10.1016/J.FEBSLET.2015.11.030 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.9 Å) |
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