5fh9

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

spinqualitylabelsall models 5fh9, resolution 3.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fh9 is a 2 chain structure with sequence from Bacillus sp. SH51. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.159Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function J7QA66_ECOLX Fe(2+) uptake system, probably driven by GTP.[RuleBase:RU362098] Publication Abstract from PubMed 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. Studies on the X-Ray and Solution Structure of FeoB from Escherichia coli BL21.,Hagelueken G, Hoffmann J, Schubert E, Duthie FG, Florin N, Konrad L, Imhof D, Behrmann E, Morgner N, Schiemann O Biophys J. 2016 Jun 21;110(12):2642-50. doi: 10.1016/j.bpj.2016.05.018. PMID:27332122 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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