2fl0

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(New page: 200px<br /><applet load="2fl0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fl0, resolution 2.70&Aring;" /> '''Oxidized (All ferric...)
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[[Image:2fl0.gif|left|200px]]<br /><applet load="2fl0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2fl0, resolution 2.70&Aring;" />
 
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'''Oxidized (All ferric) form of the Azotobacter vinelandii bacterioferritin'''<br />
 
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==Overview==
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==Oxidized (All ferric) form of the Azotobacter vinelandii bacterioferritin==
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In this work, we report the X-ray crystal structure of the aerobically, isolated (oxidized) and the anaerobic dithionite-reduced (at pH 8.0) forms, of the native Azotobacter vinelandii bacterioferritin to 2.7 and 2.0 A, resolution, respectively. Iron K-edge multiple anomalous dispersion (MAD), experiments unequivocally identified the presence of three independent, iron-containing sites within the protein structure. Specifically, a, dinuclear (ferroxidase) site, a b-type heme site, and the binding of a, single iron atom at the four-fold molecular axis of the protein shell were, observed. In addition to the novel observation of iron at the four-fold, pore, these data also reveal that the oxidized form of the protein has a, symmetrical ferroxidase site containing two five-coordinate iron atoms., Each iron atom is ligated by four carboxylate oxygen atoms and a single, histidyl nitrogen atom. A single water molecule is found within hydrogen, bonding distance of the ferroxidase site that bridges the two iron atoms, on the side opposite the histidine ligands. Chemical reduction of the, protein under anaerobic conditions results in an increase in the average, Fe-Fe distance in the ferroxidase site from approximately 3.5 to, approximately 4.0 A and the loss of one of the ligands, H130. In addition, there is significant movement of the bridging water molecule and several, other amino acid side chains in the vicinity of the ferroxidase site and, along the D helix to the three-fold symmetry axis. In contrast to previous, work, the higher-resolution data for the dithionite-reduced structure, suggest that the heme may be bound in multiple conformations. Taken, together, these data allow a molecular movie of the ferroxidase gating, mechanism to be developed and provide further insight into the iron uptake, and/or release and mineralization mechanism of bacterioferritins in, general.
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<StructureSection load='2fl0' size='340' side='right'caption='[[2fl0]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2fl0]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FL0 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fl0 OCA], [https://pdbe.org/2fl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fl0 RCSB], [https://www.ebi.ac.uk/pdbsum/2fl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fl0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BFR_AZOVI BFR_AZOVI] 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 (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fl/2fl0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2fl0 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2FL0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with FE2, MG and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FL0 OCA].
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*[[Ferritin 3D structures|Ferritin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Redox-dependent structural changes in the Azotobacter vinelandii bacterioferritin: new insights into the ferroxidase and iron transport mechanism., Swartz L, Kuchinskas M, Li H, Poulos TL, Lanzilotta WN, Biochemistry. 2006 Apr 11;45(14):4421-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16584178 16584178]
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[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kunchinskas, K.]]
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[[Category: Kunchinskas K]]
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[[Category: Lanzilotta, W.N.]]
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[[Category: Lanzilotta WN]]
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[[Category: Li, H.]]
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[[Category: Li H]]
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[[Category: Poulos, T.L.]]
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[[Category: Poulos TL]]
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[[Category: Swartz, L.]]
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[[Category: Swartz L]]
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[[Category: FE2]]
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[[Category: HEM]]
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[[Category: MG]]
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[[Category: bacterioferritin]]
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[[Category: diiron site]]
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[[Category: ferritin]]
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[[Category: iron transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:36:48 2007''
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Current revision

Oxidized (All ferric) form of the Azotobacter vinelandii bacterioferritin

PDB ID 2fl0

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