5WUQ
Crystal structure of SigW in complex with its anti-sigma RsiW, a zinc binding form
5WUQ の概要
エントリーDOI | 10.2210/pdb5wuq/pdb |
関連するPDBエントリー | 5WUR |
分子名称 | ECF RNA polymerase sigma factor SigW, Anti-sigma-W factor RsiW, ZINC ION (3 entities in total) |
機能のキーワード | sigma-anti-sigma complex, zinc binding motif, metal binding protein |
由来する生物種 | Bacillus subtilis subsp. subtilis str. 168 詳細 |
細胞内の位置 | Membrane ; Single-pass membrane protein : Q45588 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 62058.89 |
構造登録者 | |
主引用文献 | Devkota, S.R.,Kwon, E.,Ha, S.C.,Chang, H.W.,Kim, D.Y. Structural insights into the regulation of Bacillus subtilis SigW activity by anti-sigma RsiW PLoS ONE, 12:e0174284-e0174284, 2017 Cited by PubMed Abstract: Bacillus subtilis SigW is localized to the cell membrane and is inactivated by the tight interaction with anti-sigma RsiW under normal growth conditions. Whereas SigW is discharged from RsiW binding and thus initiates the transcription of its regulon under diverse stress conditions such as antibiotics and alkaline shock. The release and activation of SigW in response to extracytoplasmic signals is induced by the regulated intramembrane proteolysis of RsiW. As a ZAS (Zinc-containing anti-sigma) family protein, RsiW has a CHCC zinc binding motif, which implies that its anti-sigma activity may be regulated by the state of zinc coordination in addition to the proteolytic cleavage of RsiW. To understand the regulation mode of SigW activity by RsiW, we determined the crystal structures of SigW in complex with the cytoplasmic domain of RsiW, and compared the conformation of the CHCC motif in the reduced/zinc binding and the oxidized states. The structures revealed that RsiW inhibits the promoter binding of SigW by interacting with the surface groove of SigW. The interaction between SigW and RsiW is not disrupted by the oxidation of the CHCC motif in RsiW, suggesting that SigW activity might not be regulated by the zinc coordination states of the CHCC motif. PubMed: 28319136DOI: 10.1371/journal.pone.0174284 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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