1xoa: Difference between revisions
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'''THIOREDOXIN (OXIDIZED DISULFIDE FORM), NMR, 20 STRUCTURES''' | {{Structure | ||
|PDB= 1xoa |SIZE=350|CAPTION= <scene name='initialview01'>1xoa</scene> | |||
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'''THIOREDOXIN (OXIDIZED DISULFIDE FORM), NMR, 20 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1XOA is a [ | 1XOA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOA OCA]. | ||
==Reference== | ==Reference== | ||
High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin., Jeng MF, Campbell AP, Begley T, Holmgren A, Case DA, Wright PE, Dyson HJ, Structure. 1994 Sep 15;2(9):853-68. PMID:[http:// | High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin., Jeng MF, Campbell AP, Begley T, Holmgren A, Case DA, Wright PE, Dyson HJ, Structure. 1994 Sep 15;2(9):853-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7812718 7812718] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: redox-active center]] | [[Category: redox-active center]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:12:26 2008'' | ||
Revision as of 16:12, 20 March 2008
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THIOREDOXIN (OXIDIZED DISULFIDE FORM), NMR, 20 STRUCTURES
OverviewOverview
BACKGROUND: Thioredoxin participates in thiol-disulfide exchange reactions and both oxidized thioredoxin (disulfide form) and reduced thioredoxin (dithiol form) are found under physiological conditions. Previous structural studies suggested that the two forms were extremely similar, although significant functional and spectroscopic differences exist. We therefore undertook high-resolution solution structural studies of the two forms of Escherichia coli thioredoxin in order to detect subtle conformational differences. RESULTS: The solution structures of reduced and oxidized thioredoxin are extremely similar. Backbone structure is largely identical in the two forms, with slight differences in the region of the active site, which includes Cys32 and Cys35. The side chain sulfur atom of Cys32 is tilted away from that of Cys35 in the reduced form of the protein to accommodate the increase in S-S distance that occurs upon reduction of the disulfide, but the chi 1 angles of the two cysteines remain the same in the two forms. CONCLUSIONS: Only subtle conformational changes occur upon changing the oxidation state of the active site cysteines, including the positions of some side chains and in hydrogen bonding patterns in the active site region. Functional differences between the two forms are probably therefore related to differences in local conformational flexibility in and near the active site loop.
About this StructureAbout this Structure
1XOA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin., Jeng MF, Campbell AP, Begley T, Holmgren A, Case DA, Wright PE, Dyson HJ, Structure. 1994 Sep 15;2(9):853-68. PMID:7812718
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