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4YNL

Crystal structure of the hood domain of Anabaena HetR in complex with the hexapeptide ERGSGR derived from PatS

4YNL の概要
エントリーDOI10.2210/pdb4ynl/pdb
関連するPDBエントリー4YRV
分子名称Heterocyst differentiation control protein, Heterocyst inhibition-signaling peptide (3 entities in total)
機能のキーワードheterocyst differentiation, transcription factor, transcription
由来する生物種Nostoc sp. PCC 7120
詳細
細胞内の位置Periplasm : O52748
タンパク質・核酸の鎖数8
化学式量合計46640.81
構造登録者
Hu, H.X.,Jiang, Y.L.,Zhao, M.X.,Zhang, C.C.,Chen, Y.,Zhou, C.Z. (登録日: 2015-03-10, 公開日: 2015-12-02, 最終更新日: 2023-11-08)
主引用文献Hu, H.X.,Jiang, Y.L.,Zhao, M.X.,Cai, K.,Liu, S.,Wen, B.,Lv, P.,Zhang, Y.,Peng, J.,Zhong, H.,Yu, H.M.,Ren, Y.M.,Zhang, Z.,Tian, C.,Wu, Q.,Oliveberg, M.,Zhang, C.C.,Chen, Y.,Zhou, C.Z.
Structural insights into HetR-PatS interaction involved in cyanobacterial pattern formation
Sci Rep, 5:16470-16470, 2015
Cited by
PubMed Abstract: The one-dimensional pattern of heterocyst in the model cyanobacterium Anabaena sp. PCC 7120 is coordinated by the transcription factor HetR and PatS peptide. Here we report the complex structures of HetR binding to DNA, and its hood domain (HetRHood) binding to a PatS-derived hexapeptide (PatS6) at 2.80 and 2.10 Å, respectively. The intertwined HetR dimer possesses a couple of novel HTH motifs, each of which consists of two canonical α-helices in the DNA-binding domain and an auxiliary α-helix from the flap domain of the neighboring subunit. Two PatS6 peptides bind to the lateral clefts of HetRHood, and trigger significant conformational changes of the flap domain, resulting in dissociation of the auxiliary α-helix and eventually release of HetR from the DNA major grove. These findings provide the structural insights into a prokaryotic example of Turing model.
PubMed: 26576507
DOI: 10.1038/srep16470
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.1 Å)
構造検証レポート
Validation report summary of 4ynl
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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