6JBX
Crystal structure of Streptococcus pneumoniae FabT in complex with DNA
6JBX の概要
| エントリーDOI | 10.2210/pdb6jbx/pdb |
| 分子名称 | Fatty acid biosynthesis transcriptional regulator, DNA (5'-D(*AP*AP*TP*AP*GP*TP*TP*TP*GP*AP*CP*TP*GP*TP*CP*AP*AP*AP*TP*TP*AP*TP*G)-3'), DNA (5'-D(*CP*AP*TP*AP*AP*TP*TP*TP*GP*AP*CP*AP*GP*TP*CP*AP*AP*AP*CP*TP*AP*TP*T)-3'), ... (5 entities in total) |
| 機能のキーワード | transcription factor, marr family, fatty acid synthesis, transcription-dna complex, transcription/dna |
| 由来する生物種 | Streptococcus pneumoniae 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 50048.15 |
| 構造登録者 | |
| 主引用文献 | Zuo, G.,Chen, Z.P.,Jiang, Y.L.,Zhu, Z.,Ding, C.,Zhang, Z.,Chen, Y.,Zhou, C.Z.,Li, Q. Structural insights into repression of the Pneumococcal fatty acid synthesis pathway by repressor FabT and co-repressor acyl-ACP. Febs Lett., 593:2730-2741, 2019 Cited by PubMed Abstract: The Streptococcus pneumoniae fatty acid synthesis (FAS) pathway is globally controlled at the transcriptional level by the repressor FabT and its co-repressor acyl carrier protein (acyl-ACP), the intermediate of phospholipid synthesis. Here, we report the crystal structure of FabT complexed with a 23-bp dsDNA, which indicates that FabT is a weak repressor with low DNA-binding affinity in the absence of acyl-ACP. Modification of ACP with a long-chain fatty acid is necessary for the formation of a stable complex with FabT, mimicked in vitro by cross-linking, which significantly elevates the DNA-binding affinity of FabT. Altogether, we propose a putative working model of gene repression under the double control of FabT and acyl-ACP, elucidating a distinct repression network for Pneumococcus to precisely coordinate FAS. PubMed: 31291684DOI: 10.1002/1873-3468.13534 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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