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3TVK

Diguanylate cyclase domain of DgcZ

3TVK の概要
エントリーDOI10.2210/pdb3tvk/pdb
関連するPDBエントリー3T9O
分子名称Diguanylate cyclase DgcZ, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one), MAGNESIUM ION, ... (5 entities in total)
機能のキーワードdiguanylate cyclase, putative zinc sensor, c-di-gmp, transferase
由来する生物種Escherichia coli
タンパク質・核酸の鎖数1
化学式量合計22737.79
構造登録者
Zaehringer, F.,Schirmer, T. (登録日: 2011-09-20, 公開日: 2012-10-03, 最終更新日: 2023-09-13)
主引用文献Zahringer, F.,Lacanna, E.,Jenal, U.,Schirmer, T.,Boehm, A.
Structure and signaling mechanism of a zinc-sensory diguanylate cyclase.
Structure, 21:1149-1157, 2013
Cited by
PubMed Abstract: Diguanylate cyclases synthesize the second messenger c-di-GMP, which in turn governs a plethora of physiological processes in bacteria. Although most diguanylate cyclases harbor sensory domains, their input signals are largely unknown. Here, we demonstrate that diguanylate cyclase DgcZ (YdeH) from Escherichia coli is regulated allosterically by zinc. Crystal structures show that the zinc ion is bound to the 3His/1Cys motif of the regulatory chemoreceptor zinc-binding domain, which mediates subunit contact within the dimeric enzyme. In vitro, zinc reversibly inhibits DgcZ with a subfemtomolar Ki constant. In vivo, bacterial biofilm formation is modulated by externally applied zinc in a DgcZ- and c-di-GMP-dependent fashion. The study outlines the structural principles of this zinc sensor. Zinc binding seems to regulate the activity of the catalytic GGDEF domains by impeding their mobility and thus preventing productive encounter of the two GTP substrates.
PubMed: 23769666
DOI: 10.1016/j.str.2013.04.026
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.8 Å)
構造検証レポート
Validation report summary of 3tvk
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2026-04-29に公開中

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