Crystal Structure of the Archaeal Heat Shock Regulator from Pyrococcus furiosus: A Molecular Chimera Representing Eukaryal and Bacterial Features
Autor: | Gudrun Vierke, Rudolf Ladenstein, Wei Liu, Michael Thomm, Ann-Kathrin Wenke |
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Rok vydání: | 2007 |
Předmět: |
Models
Molecular BAG domain Archaeal Proteins Molecular Sequence Data Static Electricity Winged Helix Crystallography X-Ray Protein Structure Secondary Evolution Molecular Protein structure Structural Biology Humans Point Mutation Amino Acid Sequence Heat shock Protein Structure Quaternary Molecular Biology Heat-Shock Proteins Palindromic sequence Coiled coil Base Sequence biology biology.organism_classification Molecular biology Pyrococcus furiosus Heat shock factor Protein Subunits Biophysics Gene Expression Regulation Archaeal Dimerization Sequence Alignment |
Zdroj: | Journal of Molecular Biology. 369:474-488 |
ISSN: | 0022-2836 |
Popis: | 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. |
Databáze: | OpenAIRE |
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