1ODV

Photoactive yellow protein 1-25 deletion mutant

Summary for 1ODV

• Entry DOI: 10.2210/pdb1odv/pdb
• Related: 1D7E 1F98 1F9I 1GSV 1GSW 1GSX 1KOU 1NWZ 2PHY 2PYP 2PYR 3PHY 3PYP
• Descriptor: PHOTOACTIVE YELLOW PROTEIN, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
• Functional Keywords: signalling, photoactivity, p-coumaric acid
• Biological source: ECTOTHIORHODOSPIRA HALOPHILA
• Total number of polymer chains: 2
• Total formula weight: 22691.63

Authors

Vreede, J.,Van Der horst, M.A.,Hellingwerf, K.J.,Crielaard, W.,Van Aalten, D.M.F. (deposition date: 2003-03-14, release date: 2003-03-18, Last modification date: 2023-12-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.14 Å)