3e1m: Difference between revisions

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[[Image:3e1m.png|left|200px]]


{{STRUCTURE_3e1m|  PDB=3e1m  |  SCENE=  }}
==Crystal structure of E. coli Bacterioferritin (BFR) obtained after soaking APO-BFR crystals for 2.5 minutes in FE2+ (2.5M FE(II)-BFR)==
 
<StructureSection load='3e1m' size='340' side='right'caption='[[3e1m]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
===Crystal structure of E. coli Bacterioferritin (BFR) obtained after soaking APO-BFR crystals for 2.5 minutes in FE2+ (2.5M FE(II)-BFR)===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3e1m]] 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=3E1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E1M FirstGlance]. <br>
{{ABSTRACT_PUBMED_19391621}}
</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>
 
<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>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e1m OCA], [https://pdbe.org/3e1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e1m RCSB], [https://www.ebi.ac.uk/pdbsum/3e1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e1m ProSAT]</span></td></tr>
[[3e1m]] is a 12 chain structure of [[Ferritin]] 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=3E1M OCA].  
</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/e1/3e1m_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=3e1m ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Ferritin|Ferritin]]
*[[Ferritin 3D structures|Ferritin 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:019391621</ref><references group="xtra"/>
__TOC__
[[Category: Escherichia coli]]
</StructureSection>
[[Category: Brun, N Le.]]
[[Category: Escherichia coli K-12]]
[[Category: Crow, A.]]
[[Category: Large Structures]]
[[Category: Lawson, T.]]
[[Category: Crow A]]
[[Category: Lewin, A.]]
[[Category: Lawson T]]
[[Category: Moore, G R.]]
[[Category: Le Brun N]]
[[Category: Bacterioferritin. rhombic dodecahedral superstructure.]]
[[Category: Lewin A]]
[[Category: Heme]]
[[Category: Moore GR]]
[[Category: Iron]]
[[Category: Iron storage]]
[[Category: Metal binding protein]]
[[Category: Metal-binding]]

Latest revision as of 12:44, 21 February 2024

Crystal structure of E. coli Bacterioferritin (BFR) obtained after soaking APO-BFR crystals for 2.5 minutes in FE2+ (2.5M FE(II)-BFR)Crystal structure of E. coli Bacterioferritin (BFR) obtained after soaking APO-BFR crystals for 2.5 minutes in FE2+ (2.5M FE(II)-BFR)

Structural highlights

3e1m is a 12 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Yang X, Le Brun NE, Thomson AJ, Moore GR, Chasteen ND. The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin. Biochemistry. 2000 Apr 25;39(16):4915-23. PMID:10769150
  2. ↑ Baaghil S, Lewin A, Moore GR, Le Brun NE. Core formation in Escherichia coli bacterioferritin requires a functional ferroxidase center. Biochemistry. 2003 Dec 2;42(47):14047-56. PMID:14636073 doi:http://dx.doi.org/10.1021/bi035253u

3e1m, resolution 2.70Å

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