2P4W

Crystal structure of heat shock regulator from Pyrococcus furiosus

Replaces:  1XNP

Summary for 2P4W

• Entry DOI: 10.2210/pdb2p4w/pdb
• Related: 1XNP
• Descriptor: Transcriptional regulatory protein arsR family, SULFATE ION (3 entities in total)
• Functional Keywords: archaea, phr, heat shock, transcriptional regulation, winged helix, dna binding, transcription
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 2
• Total formula weight: 48244.25

Authors

Liu, W.,Vierke, G.,Panjikar, S.,Thomm, M.,Ladenstein, R. (deposition date: 2007-03-13, release date: 2007-03-27, Last modification date: 2023-08-30)

Primary citation

Liu, W.,Vierke, G.,Wenke, A.K.,Thomm, M.,Ladenstein, R.
Crystal Structure of the Archaeal Heat Shock Regulator from Pyrococcus furiosus: A Molecular Chimera Representing Eukaryal and Bacterial Features.
J.Mol.Biol., 369:474-488, 2007

PubMed Abstract: We report here the crystal structure of a protein from Pyrococcus furiosus (Phr) that represents the first characterized heat shock transcription factor in archaea. Phr specifically represses the expression of heat shock genes at physiological temperature in vitro and in vivo but is released from the promoters upon heat shock response. Structure analysis revealed a stable homodimer, each subunit consisting of an N-terminal winged helix DNA-binding domain (wH-DBD) and a C-terminal antiparallel coiled coil helical domain. The overall structure shows as a molecular chimera with significant folding similarity of its DBD to the bacterial SmtB/ArsR family, while its C-terminal part was found to be a remote homologue of the eukaryotic BAG domain. The dimeric protein recognizes a palindromic DNA sequence. Molecular docking and mutational analyses suggested a novel binding mode in which the major specific contacts occur at the minor groove interacting with the strongly basic wing containing a cluster of three arginine residues.

PubMed: 17434531
DOI: 10.1016/j.jmb.2007.03.044

Experimental method

X-RAY DIFFRACTION (2.6 Å)