View source for 5fh9


==Crystal structure of NFeoB from Escherichia coli BL21 in the apo state.==
<StructureSection load='5fh9' size='340' side='right'caption='[[5fh9]], [[Resolution|resolution]] 3.16&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fh9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._SH51 Bacillus sp. SH51]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FH9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.159&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fh9 OCA], [https://pdbe.org/5fh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fh9 RCSB], [https://www.ebi.ac.uk/pdbsum/5fh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fh9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/J7QA66_ECOLX J7QA66_ECOLX] Fe(2+) uptake system, probably driven by GTP.[RuleBase:RU362098]
<div style="background-color:#fffaf0;">
== 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<ref>PMID:27332122</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fh9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus sp. SH51]]
[[Category: Large Structures]]
[[Category: Hagelueken G]]