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1Y6D

Solution structure and dynamics of LuxU from Vibrio harveyi, a phosphotransferase protein involved in bacterial quorum sensing

1Y6D の概要
エントリーDOI10.2210/pdb1y6d/pdb
分子名称Phosphorelay protein luxU (1 entity in total)
機能のキーワードphosphotransferase, four-helix bundle, quorum sensing, phosphorelay, transferase
由来する生物種Vibrio harveyi
タンパク質・核酸の鎖数1
化学式量合計13530.19
構造登録者
Ulrich, D.L.,Kojetin, D.,Bassler, B.L.,Cavanagh, J.,Loria, J.P. (登録日: 2004-12-06, 公開日: 2004-12-14, 最終更新日: 2024-05-22)
主引用文献Ulrich, D.L.,Kojetin, D.,Bassler, B.L.,Cavanagh, J.,Loria, J.P.
Solution structure and dynamics of LuxU from Vibrio harveyi, a phosphotransferase protein involved in bacterial quorum sensing.
J.Mol.Biol., 347:297-307, 2005
Cited by
PubMed Abstract: The marine bacterium Vibrio harveyi controls its bioluminescence by a process known as quorum sensing. In this process, autoinducer molecules are detected by membrane-bound sensor kinase/response regulator proteins (LuxN and LuxQ) that relay a signal via a series of protein phosphorylation reactions to another response regulator protein, LuxO. Phosphorylated LuxO indirectly represses the expression of the proteins responsible for bioluminescence. Integral to this quorum sensing process is the function of the phosphotransferase protein, LuxU. LuxU acts to shuttle the phosphate from the membrane-bound proteins, LuxN and LuxQ, to LuxO. LuxU is a 114 amino acid residue monomeric protein. Solution NMR was used to determine the three-dimensional structure of LuxU. LuxU contains a four-helix bundle topology with the active-site histidine residue (His58) located on alpha-helix C and exposed to solution. The active site represents a cluster of positively charged residues located on an otherwise hydrophobic protein face. NMR spin-relaxation experiments identify a collection of flexible residues localized on the same region of LuxU as His58. The studies described here represent the first structural characterization of an isolated, monomeric bacterial phosphotransferase protein.
PubMed: 15740742
DOI: 10.1016/j.jmb.2005.01.039
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実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1y6d
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2026-04-15に公開中

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