1xob: Difference between revisions
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'''THIOREDOXIN (REDUCED DITHIO FORM), NMR, 20 STRUCTURES''' | '''THIOREDOXIN (REDUCED DITHIO FORM), NMR, 20 STRUCTURES''' | ||
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==About this Structure== | ==About this Structure== | ||
1XOB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry | 1XOB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1trx 1trx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOB OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Jeng, M F.]] | [[Category: Jeng, M F.]] | ||
[[Category: Wright, P E.]] | [[Category: Wright, P E.]] | ||
[[Category: | [[Category: Electron transport]] | ||
[[Category: | [[Category: Redox-active center]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:17:31 2008'' | |||
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Revision as of 15:17, 3 May 2008
THIOREDOXIN (REDUCED DITHIO 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
1XOB is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1trx. 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 Page seeded by OCA on Sat May 3 15:17:31 2008