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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
2004-5-4
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pubmed:databankReference |
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pubmed:abstractText |
PAS domains, which have been identified in over 1100 proteins from all three kingdoms of life, convert various input stimuli into signals that propagate to downstream components by modifying protein-protein interactions. One such protein is the Escherichia coli redox sensor, Ec DOS, a phosphodiesterase that degrades cyclic adenosine monophosphate in a redox-dependent manner. Here we report the crystal structures of the heme PAS domain of Ec DOS in both inactive Fe(3+) and active Fe(2+) forms at 1.32 and 1.9 A resolution, respectively. The protein folds into a characteristic PAS domain structure and forms a homodimer. In the Fe(3+) form, the heme iron is ligated to a His-77 side chain and a water molecule. Heme iron reduction is accompanied by heme-ligand switching from the water molecule to a side chain of Met-95 from the FG loop. Concomitantly, the flexible FG loop is significantly rigidified, along with a change in the hydrogen bonding pattern and rotation of subunits relative to each other. The present data led us to propose a novel redox-regulated molecular switch in which local heme-ligand switching may trigger a global "scissor-type" subunit movement that facilitates catalytic control.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20186-93
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:14982921-Amino Acid Sequence,
pubmed-meshheading:14982921-Carrier Proteins,
pubmed-meshheading:14982921-Catalysis,
pubmed-meshheading:14982921-Crystallography, X-Ray,
pubmed-meshheading:14982921-Cyclic AMP,
pubmed-meshheading:14982921-Dimerization,
pubmed-meshheading:14982921-Escherichia coli,
pubmed-meshheading:14982921-Escherichia coli Proteins,
pubmed-meshheading:14982921-Heme,
pubmed-meshheading:14982921-Hydrogen Bonding,
pubmed-meshheading:14982921-Iron,
pubmed-meshheading:14982921-Ligands,
pubmed-meshheading:14982921-Methionine,
pubmed-meshheading:14982921-Models, Molecular,
pubmed-meshheading:14982921-Molecular Sequence Data,
pubmed-meshheading:14982921-Oxidation-Reduction,
pubmed-meshheading:14982921-Phosphoric Diester Hydrolases,
pubmed-meshheading:14982921-Protein Folding,
pubmed-meshheading:14982921-Protein Structure, Tertiary,
pubmed-meshheading:14982921-Sequence Homology, Amino Acid
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pubmed:year |
2004
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pubmed:articleTitle |
A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor.
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pubmed:affiliation |
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi 980-8577, Japan. kurokawa@tagen.tohoku.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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