View source for 3e1q


==Crystal structure of W133F variant E. coli Bacterioferritn with iron.==
<StructureSection load='3e1q' size='340' side='right'caption='[[3e1q]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3e1q]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E1Q 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3e1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1q OCA], [https://pdbe.org/3e1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e1q RCSB], [https://www.ebi.ac.uk/pdbsum/3e1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e1q ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BFR_ECOLI BFR_ECOLI] Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.<ref>PMID:10769150</ref> <ref>PMID:14636073</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e1/3e1q_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3e1q ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ferritins solubilize and detoxify the essential metal iron through formation of a ferric mineral within the protein's central cavity. Key to this activity is an intrasubunit catalytic dinuclear iron center called the ferroxidase center. Here we show that the fluorescence intensity of Escherichia coli bacterioferritin (BFR), due to the presence of two tryptophan residues (Trp35 and Trp133) in each of the 24 subunits, is highly sensitive to the iron status of the ferroxidase center and is quenched to different extents by Fe2+ and Fe3+. Recovery of the quench following oxidation of Fe2+ to Fe3+ at the ferroxidase center was not observed, indicating that the di-Fe3+ form of the center is stable. Studies of the single-tryptophan variants W35F and W133F showed that Trp133, which lies approximately 10 A from the ferroxidase center, is primarily responsible for the observed fluorescence sensitivity to iron, while studies of a stable E. coli BFR subunit dimer demonstrated that the observed quench properties are principally derived from the interaction of iron with tryptophan residues within the subunit dimer. A double-tryptophan variant (W35F/W133F) was found to exhibit fluorescence from the seven tyrosine residues present in each subunit, which was also sensitive to the iron status of the ferroxidase center. Finally, we demonstrate using Zn2+, a potent competitive inhibitor of Fe2+ binding and oxidation, that the fluorescence response can be used to monitor the loss of iron from the ferroxidase center.

Monitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopy.,Lawson TL, Crow A, Lewin A, Yasmin S, Moore GR, Le Brun NE Biochemistry. 2009 Sep 29;48(38):9031-9. PMID:19705876<ref>PMID:19705876</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3e1q" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ferritin 3D structures|Ferritin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Crow A]]
[[Category: Lawson TL]]
[[Category: Le Brun NE]]
[[Category: Lewin A]]
[[Category: Moore GR]]