Structural highlights
Function
[GLRX5_YEAST] Monothiol glutaredoxin involved in iron-sulfur biogenesis. Required for normal iron homeostasis. Protects cells against oxidative damage due to reactive oxygen species.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Grx5 from the yeast Saccharomyces cerevisiae is a monothiol glutaredoxin that is involved in iron-sulfur cluster biogenesis. Here, yeast Grx5 was cloned and overproduced in Escherichia coli. The purified protein was crystallized using the hanging-drop vapour-diffusion method. Diffraction data for Grx5 were collected to 1.67 A resolution. The crystal of Grx5 belonged to space group R3, with unit-cell parameters a = b = 85.12, c = 48.95 A, alpha = beta = 90.00, gamma = 120.00 degrees .
Cloning, overproduction, purification, crystallization and preliminary X-ray diffraction analysis of yeast glutaredoxin Grx5.,Wang Y, He YX, Yu J, Zhou CZ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jun 1;65(Pt, 6):651-3. Epub 2009 May 23. PMID:19478456[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rodriguez-Manzaneque MT, Tamarit J, Belli G, Ros J, Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol Biol Cell. 2002 Apr;13(4):1109-21. PMID:11950925 doi:http://dx.doi.org/10.1091/mbc.01-10-0517
- ↑ Wang Y, He YX, Yu J, Zhou CZ. Cloning, overproduction, purification, crystallization and preliminary X-ray diffraction analysis of yeast glutaredoxin Grx5. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jun 1;65(Pt, 6):651-3. Epub 2009 May 23. PMID:19478456 doi:10.1107/S1744309109018417
