1FOV

GLUTAREDOXIN 3 FROM ESCHERICHIA COLI IN THE FULLY OXIDIZED FORM

Summary for 1FOV

• Entry DOI: 10.2210/pdb1fov/pdb
• Related: 3GRX
• NMR Information: BMRB: 4850
• Descriptor: GLUTAREDOXIN 3 (1 entity in total)
• Functional Keywords: active site disulfide, cis pro 53, electron transport
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 9079.34

Authors

Nordstrand, K.,Sandstrom, A.,Aslund, F.,Holmgren, A.,Otting, G.,Berndt, K.D. (deposition date: 2000-08-29, release date: 2000-10-26, Last modification date: 2024-10-30)

Primary citation

Nordstrand, K.,Sandstrom, A.,Aslund, F.,Holmgren, A.,Otting, G.,Berndt, K.D.
NMR structure of oxidized glutaredoxin 3 from Escherichia coli.
J.Mol.Biol., 303:423-432, 2000

PubMed Abstract: 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.

PubMed: 11031118
DOI: 10.1006/jmbi.2000.4145

Experimental method

SOLUTION NMR