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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DOI10.2210/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
Hong, E.,Lee, W. (登録日: 2006-07-19, 公開日: 2007-05-08, 最終更新日: 2024-05-01)
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: 17491010
DOI: 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
Validation report summary of 2hqn
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2026-04-22に公開中

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