2A02

Solution NMR Structure of the Periplasmic Signaling Domain of the Outer Membrane Iron Transporter PupA from Pseudomonas putida.

2A02 の概要

• エントリーDOI: 10.2210/pdb2a02/pdb
• 関連するPDBエントリー: 1ZZV
• 分子名称: Ferric-pseudobactin 358 receptor (1 entity in total)
• 機能のキーワード: membrane protein, metal transport, protein nmr
• 由来する生物種: Pseudomonas putida
• 細胞内の位置: Cell outer membrane: P25184
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8751.72

構造登録者

Ferguson, A.D.,Amezcua, C.A.,Chelliah, Y.,Rosen, M.K.,Deisenhofer, J. (登録日: 2005-06-15, 公開日: 2006-09-26, 最終更新日: 2024-05-22)

主引用文献

Ferguson, A.D.,Amezcua, C.A.,Halabi, N.M.,Chelliah, Y.,Rosen, M.K.,Ranganathan, R.,Deisenhofer, J.
Signal transduction pathway of TonB-dependent transporters.
Proc.Natl.Acad.Sci.Usa, 2:513-518, 2006

PubMed Abstract: Transcription of the ferric citrate import system is regulated by ferric citrate binding to the outer membrane transporter FecA. A signal indicating transporter occupancy is relayed across the outer membrane to energy-transducing and regulatory proteins embedded in the cytoplasmic membrane. Because transcriptional activation is not coupled to ferric citrate import, an allosteric mechanism underlies this complex signaling mechanism. Using evolution-based statistical analysis we have identified a sparse but structurally connected network of residues that links distant functional sites in FecA. Functional analyses of these positions confirm their involvement in the mechanism that regulates transcriptional activation in response to ferric citrate binding at the cell surface. This mechanism appears to be conserved and provides the structural basis for the allosteric signaling of TonB-dependent transporters.

PubMed: 17197416
DOI: 10.1073/pnas.0609887104

実験手法

SOLUTION NMR