4ELY の概要
エントリーDOI | 10.2210/pdb4ely/pdb |
関連するPDBエントリー | 3JRZ 3JSC 4elz |
分子名称 | DNA gyrase subunit A, CcdB, SULFATE ION, ... (5 entities in total) |
機能のキーワード | alpha+beta, topoisomerase, toxin-isomerase complex, toxin/isomerase |
由来する生物種 | Shigella flexneri 詳細 |
細胞内の位置 | Cytoplasm (Potential): P0AES5 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 59060.46 |
構造登録者 | De Jonge, N.,Simic, R.,Buts, L.,Haesaerts, S.,Roelants, K.,Garcia-Pino, A.,Sterckx, Y.,De Greve, H.,Lah, J.,Loris, R. (登録日: 2012-04-11, 公開日: 2012-05-30, 最終更新日: 2023-09-13) |
主引用文献 | De Jonge, N.,Simic, M.,Buts, L.,Haesaerts, S.,Roelants, K.,Garcia-Pino, A.,Sterckx, Y.,De Greve, H.,Lah, J.,Loris, R. Alternative interactions define gyrase specificity in the CcdB family. Mol.Microbiol., 84:965-978, 2012 Cited by PubMed Abstract: Toxin-antitoxin (TA) modules are small operons associated with stress response of bacteria. F-plasmid CcdB(F) was the first TA toxin for which its target, gyrase, was identified. Plasmidic and chromosomal CcdBs belong to distinct families. Conserved residues crucial for gyrase poisoning activity of plasmidic CcdBs are not conserved among these families. Here we show that the chromosomal CcdB(Vfi) from Vibrio fischeri is an active gyrase poison that interacts with its target via an alternative energetic mechanism. Changes in the GyrA14-binding surface of the Vibrio and F-plasmid CcdB family members illustrate neutral drift where alternative interactions can be used to achieve the same functionality. Differences in affinity between V. fischeri and F-plasmid CcdB for gyrase and their corresponding CcdA antitoxin possibly reflect distinct roles for TA modules located on plasmids and chromosomes. PubMed: 22582791DOI: 10.1111/j.1365-2958.2012.08069.x 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.932 Å) |
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