Motion in Thioredoxin reductase/Glutathione reductase [reduct]

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Classification Known Domain Motion, Hinge Mechanism [D-h-2]

Structures
1TDE Unbound [ PartsList ]
1F6M AADP+ bound

Description
Comparison of two indicates large conformational change involving 66 degree rotation of one domain

Particular values describing motion
Creation Date = 19970822
Modification Date = 19970822
Experimental Methods = x (Traditional x-ray)

References
Lennon BW, Williams CH Jr, Ludwig ML. Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase. Science. 2000 Aug 18;289(5482):1190-4. [Medline info for 10947986]
G Waksman, T S Krishna, C Williams, Jr. and J Kuriyan (1994). Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis. J Mol Biol. 236: 800-816. [Medline info for 94157914]

GO terms associated with structures
Molecular functionoxidoreductase activity, thioredoxin-disulfide reductase activity, electron transporter activity, disulfide oxidoreductase activity
Cellular componentcytoplasm
Biological processremoval of superoxide radicals, electron transport

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
Thioredoxin Reductase (E.C. 1. 1tde [ A ] 1f6m [ E ] 320


Automatic morphs
Morph Morph name Structure #1 Structure #2 Residues
Thioredoxin Reductase 1f6m [ B ] 1tde [ A ] 316
Thioredoxin Reductase 1f6m [ F ] 1tde [ A ] 316
Thioredoxin Reductase 1f6m [ B ] 1tdf [ A ] 316
Thioredoxin Reductase 1f6m [ F ] 1tdf [ A ] 316
Thioredoxin Reductase (E.C. 1. 1tde [ A ] 1f6m [ A ] 320
Thioredoxin Reductase (E.C. 1. 1tdf [ A ] 1f6m [ E ] 320
Thioredoxin Reductase (E.C. 1. 1tdf [ A ] 1f6m [ A ] 320

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu