2JEE
Xray structure of E. coli YiiU
2JEE の概要
エントリーDOI | 10.2210/pdb2jee/pdb |
分子名称 | CELL DIVISION PROTEIN ZAPB (2 entities in total) |
機能のキーワード | ftsz, septum, coiled-coil, cell division, cell cycle, hypothetical protein |
由来する生物種 | ESCHERICHIA COLI |
細胞内の位置 | Cytoplasm: P0AF36 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 38583.12 |
構造登録者 | |
主引用文献 | Ebersbach, G.,Galli, E.,Moller-Jensen, J.,Lowe, J.,Gerdes, K. Novel Coiled-Coil Cell Division Factor Zapb Stimulates Z Ring Assembly and Cell Division. Mol.Microbiol., 68:720-, 2008 Cited by PubMed Abstract: Formation of the Z ring is the first known event in bacterial cell division. However, it is not yet known how the assembly and contraction of the Z ring are regulated. Here, we identify a novel cell division factor ZapB in Escherichia coli that simultaneously stimulates Z ring assembly and cell division. Deletion of zapB resulted in delayed cell division and the formation of ectopic Z rings and spirals, whereas overexpression of ZapB resulted in nucleoid condensation and aberrant cell divisions. Localization of ZapB to the divisome depended on FtsZ but not FtsA, ZipA or FtsI, and ZapB interacted with FtsZ in a bacterial two-hybrid analysis. The simultaneous inactivation of FtsA and ZipA prevented Z ring assembly and ZapB localization. Time lapse microscopy showed that ZapB-GFP is present at mid-cell in a pattern very similar to that of FtsZ. Cells carrying a zapB deletion and the ftsZ84(ts) allele exhibited a synthetic sick phenotype and aberrant cell divisions. The crystal structure showed that ZapB exists as a dimer that is 100% coiled-coil. In vitro, ZapB self-assembled into long filaments and bundles. These results raise the possibility that ZapB stimulates Z ring formation directly via its capacity to self-assemble into larger structures. PubMed: 18394147DOI: 10.1111/J.1365-2958.2008.06190.X 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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