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3BRE

Crystal Structure of P.aeruginosa PA3702

3BRE の概要
エントリーDOI10.2210/pdb3bre/pdb
分子名称Probable two-component response regulator, MAGNESIUM ION, 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) (3 entities in total)
機能のキーワードprotein-nucleotide complex, signaling protein
由来する生物種Pseudomonas aeruginosa
タンパク質・核酸の鎖数2
化学式量合計81236.75
構造登録者
De, N.,Pirruccello, M.,Krasteva, P.V.,Bae, N.,Raghavan, R.V.,Sondermann, H. (登録日: 2007-12-21, 公開日: 2008-04-01, 最終更新日: 2023-08-30)
主引用文献De, N.,Pirruccello, M.,Krasteva, P.V.,Bae, N.,Raghavan, R.V.,Sondermann, H.
Phosphorylation-independent regulation of the diguanylate cyclase WspR.
Plos Biol., 6:e67-e67, 2008
Cited by
PubMed Abstract: Environmental signals that trigger bacterial pathogenesis and biofilm formation are mediated by changes in the level of cyclic dimeric guanosine monophosphate (c-di-GMP), a unique eubacterial second messenger. Tight regulation of cellular c-di-GMP concentration is governed by diguanylate cyclases and phosphodiesterases, which are responsible for its production and degradation, respectively. Here, we present the crystal structure of the diguanylate cyclase WspR, a conserved GGDEF domain-containing response regulator in Gram-negative bacteria, bound to c-di-GMP at an inhibitory site. Biochemical analyses revealed that feedback regulation involves the formation of at least three distinct oligomeric states. By switching from an active to a product-inhibited dimer via a tetrameric assembly, WspR utilizes a novel mechanism for modulation of its activity through oligomerization. Moreover, our data suggest that these enzymes can be activated by phosphodiesterases. Thus, in addition to the canonical pathways via phosphorylation of the regulatory domains, both product and enzyme concentration contribute to the coordination of c-di-GMP signaling. A structural comparison reveals resemblance of the oligomeric states to assemblies of GAF domains, widely used regulatory domains in signaling molecules conserved from archaea to mammals, suggesting a similar mechanism of regulation.
PubMed: 18366254
DOI: 10.1371/journal.pbio.0060067
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4 Å)
構造検証レポート
Validation report summary of 3bre
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2026-07-08に公開中

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