2HQN
Structure of a Atypical Orphan Response Regulator Protein Revealed a New Phosphorylation-Independent Regulatory Mechanism
2HQN の概要
| エントリーDOI | 10.2210/pdb2hqn/pdb |
| 関連するPDBエントリー | 2HQO 2HQR |
| 分子名称 | Putative TRANSCRIPTIONAL REGULATOR (1 entity in total) |
| 機能のキーワード | phosporylation-independent response regulator, signaling protein |
| 由来する生物種 | Helicobacter pylori |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12481.29 |
| 構造登録者 | |
| 主引用文献 | Hong, E.,Lee, H.M.,Ko, H.,Kim, D.-U.,Jeon, B.-Y.,Jung, J.,Shin, J.,Lee, S.-A.,Kim, Y.,Jeon, Y.H.,Cheong, C.,Cho, H.-S.,Lee, W. Structure of an Atypical Orphan Response Regulator Protein Supports a New Phosphorylation-independent Regulatory Mechanism J.Biol.Chem., 282:20667-20675, 2007 Cited by PubMed Abstract: Two-component signal transduction systems, commonly found in prokaryotes, typically regulate cellular functions in response to environmental conditions through a phosphorylation-dependent process. A new type of response regulator, hp1043 (HP-RR) from Helicobacter pylori, has been recently identified. HP-RR is essential for cell growth and does not require the well known phosphorelay scheme. Unphosphorylated HP-RR binds specifically to its own promoter (P(1043)) and autoregulates the promoter of the tlpB gene (P(tlpB)). We have determined the structure of HP-RR by NMR and x-ray crystallography, revealing a symmetrical dimer with two functional domains. The molecular topology resembles that of the OmpR/PhoB subfamily, however, the symmetrical dimer is stable even in the unphosphorylated state. The dimer interface, formed by three secondary structure elements (alpha4-beta5-alpha5), resembles that of the active, phosphorylated forms of ArcA and PhoB. Several conserved residues of the HP-RR dimeric interface deviate from the OmpR/PhoB subfamily, although there are similar salt bridges and hydrophobic patches within the interface. Our findings reveal how a new type of response regulator protein could function as a cell growth-associated regulator in the absence of post-translational modification. PubMed: 17491010DOI: 10.1074/jbc.M609104200 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
構造検証レポート
検証レポート(詳細版)
をダウンロード






