5FH9

Crystal structure of NFeoB from Escherichia coli BL21 in the apo state.

5FH9 の概要

• エントリーDOI: 10.2210/pdb5fh9/pdb
• 分子名称: Ferrous iron transport protein B (1 entity in total)
• 機能のキーワード: gtpase, metal transport
• 由来する生物種: Escherichia coli BL21
• 細胞内の位置: Cell inner membrane : J7QA66
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60140.70

構造登録者

Hagelueken, G. (登録日: 2015-12-21, 公開日: 2016-07-27, 最終更新日: 2024-05-08)

主引用文献

Hagelueken, G.,Hoffmann, J.,Schubert, E.,Duthie, F.G.,Florin, N.,Konrad, L.,Imhof, D.,Behrmann, E.,Morgner, N.,Schiemann, O.
Studies on the X-Ray and Solution Structure of FeoB from Escherichia coli BL21.
Biophys.J., 110:2642-2650, 2016

PubMed Abstract: The ferrous iron transporter FeoB is an important factor in the iron metabolism of many bacteria. Although several structural studies have been performed on its cytosolic GTPase domain (NFeoB), the full-length structure of FeoB remains elusive. Based on a crystal packing analysis that was performed on crystals of NFeoB, a trimeric structure of the FeoB channel was proposed, where the transport pore runs along the trimer axis. Because this trimer has not been observed in some subsequently solved structures of NFeoB homologs, it remains unclear whether or not the trimer is indeed functionally relevant. Here, pulsed electron-electron double resonance spectroscopy, negative stain electron microscopy, and native mass spectrometry are used to analyze the oligomeric state of different soluble and full-length FeoB constructs. The results show that the full-length protein is predominantly monomeric, whereas dimers and trimers are formed to a small percentage. Furthermore, the solution structure of the switch I region is analyzed by pulsed electron-electron double resonance spectroscopy and a new, to our knowledge, crystal structure of NFeoB from Escherichia coli BL21 is presented.

PubMed: 27332122
DOI: 10.1016/j.bpj.2016.05.018

実験手法

X-RAY DIFFRACTION (3.159 Å)