1ODV

Photoactive yellow protein 1-25 deletion mutant

1ODV の概要

• エントリーDOI: 10.2210/pdb1odv/pdb
• 関連するPDBエントリー: 1D7E 1F98 1F9I 1GSV 1GSW 1GSX 1KOU 1NWZ 2PHY 2PYP 2PYR 3PHY 3PYP
• 分子名称: PHOTOACTIVE YELLOW PROTEIN, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
• 機能のキーワード: signalling, photoactivity, p-coumaric acid
• 由来する生物種: ECTOTHIORHODOSPIRA HALOPHILA
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22691.63

構造登録者

Vreede, J.,Van Der horst, M.A.,Hellingwerf, K.J.,Crielaard, W.,Van Aalten, D.M.F. (登録日: 2003-03-14, 公開日: 2003-03-18, 最終更新日: 2023-12-13)

主引用文献

Vreede, J.,Van Der Horst, M.A.,Hellingwerf, K.J.,Crielaard, W.,Van Aalten, D.M.F.
Pas Domains.Common Structure and Common Flexibility
J.Biol.Chem., 278:18434-, 2003

PubMed Abstract: PAS (PER-ARNT-SIM) domains are a family of sensor protein domains involved in signal transduction in a wide range of organisms. Recent structural studies have revealed that these domains contain a structurally conserved alpha/beta-fold, whereas almost no conservation is observed at the amino acid sequence level. The photoactive yellow protein, a bacterial light sensor, has been proposed as the PAS structural prototype yet contains an N-terminal helix-turn-helix motif not found in other PAS domains. Here we describe the atomic resolution structure of a photoactive yellow protein deletion mutant lacking this motif, revealing that the PAS domain is indeed able to fold independently and is not affected by the removal of these residues. Computer simulations of currently known PAS domain structures reveal that these domains are not only structurally conserved but are also similar in their conformational flexibilities. The observed motions point to a possible common mechanism for communicating ligand binding/activation to downstream transducer proteins.

PubMed: 12639952
DOI: 10.1074/JBC.M301701200

実験手法

X-RAY DIFFRACTION (1.14 Å)