1MY6

The 1.6 A Structure of Fe-Superoxide Dismutase from the thermophilic cyanobacterium Thermosynechococcus elongatus : Correlation of EPR and Structural Characteristics

Summary for 1MY6

• Entry DOI: 10.2210/pdb1my6/pdb
• Descriptor: Iron (III) Superoxide Dismutase, FE (III) ION (3 entities in total)
• Functional Keywords: iron speroxide dismutase, thermophile, reactive oxygen species, cyanobacteria, thermosynechococcus, thermosynechococcus elongatus, superoxide dismutase, sod, fesod, iron(iii) superoxide dismutase, oxidoreductase
• Biological source: Thermosynechococcus elongatus
• Total number of polymer chains: 2
• Total formula weight: 44324.89

Authors

Yoshida, S.M.,Cascio, D.,Sawaya, M.R.,Yeates, T.O.,Kerfeld, C.A. (deposition date: 2002-10-03, release date: 2003-07-29, Last modification date: 2024-02-14)

Primary citation

Kerfeld, C.A.,Yoshida, S.,Tran, K.T.,Yeates, T.O.,Cascio, D.,Bottin, H.,Berthomieu, C.,Sugiura, M.,Boussac, A.
The 1.6 A resolution structure of Fe-superoxide dismutase from the thermophilic cyanobacterium Thermosynechococcus elongatus.
J.BIOL.INORG.CHEM., 8:707-714, 2003

PubMed Abstract: The iron-containing superoxide dismutase (FeSOD) from the thermophilic cyanobacterium Thermosynechococcus elongatus has been isolated. The protein crystallizes readily and we have determined the structure to 1.6 A resolution. This is the first structural characterization of an FeSOD isolated from a cyanobacterium and one of the highest resolution FeSOD structures determined to date. The activity of the T. elongatus FeSOD has been measured both at 25 degrees C and 50 degrees C and it has been spectroscopically characterized. The T. elongatus FeSOD EPR spectra at pH 5.1, 7.5 and 10.0 are similar. This indicates that no change in the geometry of the Fe(III) site occurs over a wide range of pH. This is in contrast to the other FeSODs described in the literature.

PubMed: 12827458
DOI: 10.1007/s00775-003-0469-0

Experimental method

X-RAY DIFFRACTION (1.6 Å)