3BRE
Crystal Structure of P.aeruginosa PA3702
3BRE の概要
| エントリーDOI | 10.2210/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: 18366254DOI: 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) |
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