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Journal article

Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria.

Abstract:

Human mitochondrial glutaredoxin 2 (GLRX2), which controls intracellular redox balance and apoptosis, exists in a dynamic equilibrium of enzymatically active monomers and quiescent dimers. Crystal structures of both monomeric and dimeric forms of human GLRX2 reveal a distinct glutathione binding mode and show a 2Fe-2S-bridged dimer. The iron-sulfur cluster is coordinated through the N-terminal active site cysteine, Cys-37, and reduced glutathione. The structures indicate that the enzyme can b...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m608179200

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Role:
Author
Journal:
The Journal of biological chemistry
Volume:
282
Issue:
5
Pages:
3077-3082
Publication date:
2007-02-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:5e047d41-3e05-4eea-bcba-d004d2ff5211
Source identifiers:
33676
Local pid:
pubs:33676

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