PDBsum entry 5fh9

Metal transport

PDB id: 5fh9

Contents

Protein chains

264 a.a.

PDB id:

5fh9

Name:

Metal transport

Title:

Crystal structure of nfeob from escherichia coli bl21 in the apo state.

Structure:

Ferrous iron transport protein b. Chain: a, b. Engineered: yes

Source:

Escherichia coli bl21. Organism_taxid: 511963. Gene: feob. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

3.16Å R-factor: 0.209 R-free: 0.228

Authors:

G.Hagelueken

Key ref:

G.Hagelueken et al. (2016). Studies on the X-Ray and Solution Structure of FeoB from Escherichia coli BL21. Biophys J, 110, 2642-2650. PubMed id: 27332122 DOI: 10.1016/j.bpj.2016.05.018

Date:

21-Dec-15 Release date: 27-Jul-16

Protein chains

J7QA66  (J7QA66_ECOLX) -  Ferrous iron transport protein B from Escherichia coli

Seq: 773 a.a.

Struc: 264 a.a.

DOI no: 10.1016/j.bpj.2016.05.018

Biophys J 110:2642-2650 (2016)

PubMed id: 27332122

Studies on the X-Ray and Solution Structure of FeoB from Escherichia coli BL21.

G.Hagelueken, J.Hoffmann, E.Schubert, F.G.Duthie, N.Florin, L.Konrad, D.Imhof, E.Behrmann, N.Morgner, O.Schiemann.

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.