The structure of an N11A mutant of the G-protein domain of FeoB
Miriam-Rose Ash, Megan J Maher, J Mitchell Guss, Mika Jormakka
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | INT UNION CRYSTALLOGRAPHY | Published : 2011
The uptake of ferrous iron in prokaryotes is mediated by the G-protein-coupled membrane protein FeoB. The protein contains two N-terminal soluble domains that are together called `NFeoB'. One of these is a G-protein domain, and GTP hydrolysis by this domain is essential for iron transport. The GTPase activity of NFeoB is accelerated in the presence of potassium ions, which bind at a site adjacent to the nucleotide. One of the ligands at the potassium-binding site is a conserved asparagine residue, which corresponds to Asn11 in Streptococcus thermophilus NFeoB. The structure of an N11A S. thermophilus NFeoB mutant has been determined and refined to a resolution of 1.85 Å; the crystals contain..View full abstract
Awarded by National Health and Medical Research Council
This study was supported by the National Health and Medical Research Council (grant Nos. 570784 and 632703). M-RA is the recipient of an Australian Postgraduate Award.