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[[Image:2htn.gif|left|200px]]
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{{STRUCTURE_2htn|  PDB=2htn  |  SCENE=  }}
'''E. coli bacterioferritin in its as-isolated form'''


==E. coli bacterioferritin in its as-isolated form==
<StructureSection load='2htn' size='340' side='right'caption='[[2htn]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2htn]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21 Escherichia coli BL21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HTN 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=2htn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2htn OCA], [https://pdbe.org/2htn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2htn RCSB], [https://www.ebi.ac.uk/pdbsum/2htn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2htn 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/ht/2htn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2htn ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Escherichia coli bacterioferritin was serendipitously crystallized in a novel cubic crystal form and its structure could be determined to 2.5 A resolution despite a high degree of merohedral twinning. This is the first report of crystallographic data on 'as-isolated' E. coli bacterioferritin. The ferroxidase active site contains positive difference density consistent with two metal ions that had co-purified with the protein. X-ray fluorescence studies suggest that the metal composition is different from that of previous structures and is a mix of zinc and native iron ions. The ferroxidase-centre configuration displays a similar flexibility as previously noted for other bacterioferritins.


==Overview==
Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form.,van Eerde A, Wolterink-van Loo S, van der Oost J, Dijkstra BW Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1061-6. Epub 2006 Oct 25. PMID:17077480<ref>PMID:17077480</ref>
Escherichia coli bacterioferritin was serendipitously crystallized in a novel cubic crystal form and its structure could be determined to 2.5 A resolution despite a high degree of merohedral twinning. This is the first report of crystallographic data on 'as-isolated' E. coli bacterioferritin. The ferroxidase active site contains positive difference density consistent with two metal ions that had co-purified with the protein. X-ray fluorescence studies suggest that the metal composition is different from that of previous structures and is a mix of zinc and native iron ions. The ferroxidase-centre configuration displays a similar flexibility as previously noted for other bacterioferritins.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2HTN is a [[Single protein]] structure of 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=2HTN OCA].
</div>
<div class="pdbe-citations 2htn" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form., van Eerde A, Wolterink-van Loo S, van der Oost J, Dijkstra BW, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1061-6. Epub 2006 Oct 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17077480 17077480]
*[[Ferritin 3D structures|Ferritin 3D structures]]
[[Category: Escherichia coli]]
== References ==
[[Category: Ferroxidase]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Dijkstra, B W.]]
</StructureSection>
[[Category: Eerde, A van.]]
[[Category: Escherichia coli BL21]]
[[Category: Loo, S Wolterink-Van.]]
[[Category: Large Structures]]
[[Category: Oost, J Van Der.]]
[[Category: Dijkstra BW]]
[[Category: Ferroxidase centre]]
[[Category: Van Der Oost J]]
[[Category: Four-helix bundle]]
[[Category: Wolterink-Van Loo S]]
[[Category: Haem]]
[[Category: Van Eerde A]]
[[Category: Iron binding site]]
[[Category: Protein shell]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:41:48 2008''
Retrieved from "https://proteopedia.org/2htn"