5FH9

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

Summary for 5FH9

• Entry DOI: 10.2210/pdb5fh9/pdb
• Descriptor: Ferrous iron transport protein B (1 entity in total)
• Functional Keywords: gtpase, metal transport
• Biological source: Escherichia coli BL21
• Cellular location: Cell inner membrane : J7QA66
• Total number of polymer chains: 2
• Total formula weight: 60140.70

Authors

Hagelueken, G. (deposition date: 2015-12-21, release date: 2016-07-27, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.159 Å)