3TAH

Crystal structure of an S. thermophilus NFeoB N11A mutant bound to mGDP

Summary for 3TAH

• Entry DOI: 10.2210/pdb3tah/pdb
• Related: 3LX5 3LX8 3SS8
• Descriptor: Ferrous iron uptake transporter protein B, 3'-O-(N-methylanthraniloyl)guanosine-5'-diphosphate, GLYCEROL, ... (5 entities in total)
• Functional Keywords: g-protein, gtpase, iron transport, potassium binding, gtp binding, metal transport
• Biological source: Streptococcus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 61773.54

Authors

Ash, M.R.,Maher, M.J.,Guss, J.M.,Jormakka, M. (deposition date: 2011-08-04, release date: 2011-12-14, Last modification date: 2023-11-01)

Primary citation

Ash, M.R.,Maher, M.J.,Guss, J.M.,Jormakka, M.
The structure of an N11A mutant of the G-protein domain of FeoB
Acta Crystallogr.,Sect.F, 67:1511-1515, 2011

PubMed Abstract: 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 contained a mixture of mant-GDP-bound and mant-GMP-bound protein. The structure demonstrates how the use of a derivatized nucleotide in cocrystallization experiments can facilitate the growth of diffraction-quality crystals.

PubMed: 22139154
DOI: 10.1107/S1744309111042965

Experimental method

X-RAY DIFFRACTION (1.85 Å)