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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 8(65), p. 784-787, 2009

DOI: 10.1107/s1744309109024464

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Crystallization and preliminary X-ray diffraction analysis of the truncated cytosolic domain of the iron transporter FeoB

Journal article published in 2009 by Yaohua Jin, Motoyuki Hattori ORCID, Hiroshi Nisimasu, Ryuichiro Ishitani, Osamu Nureki
This paper is available in a repository.
This paper is available in a repository.

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Abstract

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.