Open AccessCrystallization and preliminary X‐ray diffraction analysis of the truncated cytosolic domain of the iron transporter FeoB
Author(s) -
Jin Yaohua,
Hattori Motoyuki,
Nisimasu Hiroshi,
Ishitani Ryuichiro,
Nureki Osamu
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109024464
Subject(s) - cytosol , thermotoga maritima , thermophile , transporter , archaea , biochemistry , crystallization , bacteria , biology , chemistry , biophysics , crystallography , escherichia coli , gene , genetics , enzyme , organic chemistry
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 Å.