1bfr

<StructureSection load='1bfr' size='340' side='right' caption='[[1bfr]], [[Resolution|resolution]] 2.94&Aring;' scene=''>

<table><tr><td colspan='2'>[[1bfr]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BFR FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfr OCA], [http://pdbe.org/1bfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bfr RCSB], [http://www.ebi.ac.uk/pdbsum/1bfr PDBsum]</span></td></tr>

[[http://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>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/1bfr_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

Crystals of E. coli cytochrome b1, alias bacterioferritin, were grown fr om a low ionic strength solution. The resulting monoclniic P21 structure was solved by molecular replacement and refined using noncrystallographi c symmetries applied to the fundamental unit, consisting of two protein subunits and a single haem. From the Patterson self-rotation results it was shown that the asymmetric unit of the monoclinic crystal consists of 12 such dimers and corresponds to a complete, nearly spherical, molecule of bacterioferritin (M4 = 450 kDa) of 432 point-group symmetry. It is thus the most symmetrical cytochrome. As previously determined for the tetragonal form, the haem is located in a special position on a local twofold axis of the dimer. A bimetal centre is also observed within the four-helix bundle of each monomer; a metal-binding site is located on the fourfold axis.

Structure of a monoclinic crystal from of cyctochrome b1 (Bacterioferritin) from E. coli.,Dautant A, Meyer JB, Yariv J, Precigoux G, Sweet RM, Kalb AJ, Frolow F Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):16-24. PMID:9867433<ref>PMID:9867433</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 1bfr" style="background-color:#fffaf0;"></div>

*[[Ferritin|Ferritin]]

[[Category: Dautant, A]]

[[Category: Frolow, F]]

[[Category: Gilboa, A J.Kalb]]

[[Category: Meyer, J B]]

[[Category: Precigoux, G]]

[[Category: Sweet, R M]]

[[Category: Yariv, J]]

[[Category: Iron storage]]