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4R3A

Erythrobacter litoralis EL346 blue-light activated histidine kinase

4R3A の概要
エントリーDOI10.2210/pdb4r3a/pdb
関連するPDBエントリー4R38 4R39
分子名称Blue-light-activated histidine kinase 2, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
機能のキーワードlight-activated, lov domain, histidine kinase, bergerat fold, signal transduction, sensory transduction, photoreceptor, cell signaling, regulation, two-component system, signaling protein
由来する生物種Erythrobacter litoralis HTCC2594
タンパク質・核酸の鎖数2
化学式量合計79058.43
構造登録者
Tomchick, D.R.,Rivera-Cancel, G.,Gardner, K.H. (登録日: 2014-08-14, 公開日: 2014-12-03, 最終更新日: 2024-10-16)
主引用文献Rivera-Cancel, G.,Ko, W.H.,Tomchick, D.R.,Correa, F.,Gardner, K.H.
Full-length structure of a monomeric histidine kinase reveals basis for sensory regulation.
Proc.Natl.Acad.Sci.USA, 111:17839-17844, 2014
Cited by
PubMed Abstract: Although histidine kinases (HKs) are critical sensors of external stimuli in prokaryotes, the mechanisms by which their sensor domains control enzymatic activity remain unclear. Here, we report the full-length structure of a blue light-activated HK from Erythrobacter litoralis HTCC2594 (EL346) and the results of biochemical and biophysical studies that explain how it is activated by light. Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer. Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain. The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark. Upon light stimulation, interdomain interactions weaken to facilitate activation. Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation. We suggest parallels between EL346 and dimeric HKs, with sensor-induced movements in the DHp similarly remodeling the DHp/CA interface as part of activation.
PubMed: 25468971
DOI: 10.1073/pnas.1413983111
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.92 Å)
構造検証レポート
Validation report summary of 4r3a
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2026-04-29に公開中

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