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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2000-11-14
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pubmed:databankReference |
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pubmed:abstractText |
A high precision NMR structure of oxidized glutaredoxin 3 [C65Y] from Escherichia coli has been determined. The conformation of the active site including the disulphide bridge is highly similar to those in glutaredoxins from pig liver and T4 phage. A comparison with the previously determined structure of glutaredoxin 3 [C14S, C65Y] in a complex with glutathione reveals conformational changes between the free and substrate-bound form which includes the sidechain of the conserved, active site tyrosine residue. In the oxidized form this tyrosine is solvent exposed, while it adopts a less exposed conformation, stabilized by hydrogen bonds, in the mixed disulfide with glutathione. The structures further suggest that the formation of a covalent linkage between glutathione and glutaredoxin 3 is necessary in order to induce these structural changes upon binding of the glutathione peptide. This could explain the observed low affinity of glutaredoxins for S-blocked glutathione analogues, in spite of the fact that glutaredoxins are highly specific reductants of glutathione mixed disulfides.
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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 |
Oct
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2000 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
303
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
423-32
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11031118-Amino Acid Sequence,
pubmed-meshheading:11031118-Binding Sites,
pubmed-meshheading:11031118-Conserved Sequence,
pubmed-meshheading:11031118-Cysteine,
pubmed-meshheading:11031118-Disulfides,
pubmed-meshheading:11031118-Escherichia coli,
pubmed-meshheading:11031118-Glutaredoxins,
pubmed-meshheading:11031118-Glutathione,
pubmed-meshheading:11031118-Hydrogen Bonding,
pubmed-meshheading:11031118-Models, Molecular,
pubmed-meshheading:11031118-Molecular Sequence Data,
pubmed-meshheading:11031118-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:11031118-Oxidation-Reduction,
pubmed-meshheading:11031118-Oxidoreductases,
pubmed-meshheading:11031118-Oxygen,
pubmed-meshheading:11031118-Protein Binding,
pubmed-meshheading:11031118-Protein Conformation,
pubmed-meshheading:11031118-Proteins,
pubmed-meshheading:11031118-Reducing Agents,
pubmed-meshheading:11031118-Sequence Alignment,
pubmed-meshheading:11031118-Solvents,
pubmed-meshheading:11031118-Substrate Specificity,
pubmed-meshheading:11031118-Thermodynamics,
pubmed-meshheading:11031118-Tyrosine
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pubmed:year |
2000
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pubmed:articleTitle |
NMR structure of oxidized glutaredoxin 3 from Escherichia coli.
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pubmed:affiliation |
Center for Structural Biochemistry Karolinska Institutet, Huddinge, S-141 57, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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