Crystallization and preliminary X-ray diffraction analysis of the truncated cytosolic domain of the iron transporter FeoB.
FeoB-family proteins are widely distributed in bacteria and archaea and are involved in high-affinity Fe(2+) uptake through the plasma membrane. FeoB consists of an N-terminal cytosolic region followed by a C-terminal transmembrane region. The cytosolic region contains small GTPase and GDP dissociation inhibitor-like domains, which serve a regulatory function. The truncated cytosolic region of the iron transporter FeoB from Thermotoga maritima was overexpressed, purified and crystallized. Four native or SeMet crystal forms in a nucleotide-free state or in complex with either GDP or GMPPNP diffracted to resolutions of between 1.5 and 2.1 A.
Jin
Yaohua
Y
Department of Chemical Engineering, Tsinghua University, Beijing 100084, People's Republic of China.
Hattori
Motoyuki
M
Nisimasu
Hiroshi
H
Ishitani
Ryuichiro
R
Nureki
Osamu
O
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D003600:Cytosol / Q000737:chemistry*; D007501:Iron / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D020124:Thermotoga maritima
D001426:Bacterial Proteins; D026901:Membrane Transport Proteins; D007501:Iron