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| | ==Crystal structure of Escherichia coli bacterioferritin mutant D132F== | | ==Crystal structure of Escherichia coli bacterioferritin mutant D132F== |
| - | <StructureSection load='4u3g' size='340' side='right' caption='[[4u3g]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4u3g' size='340' side='right'caption='[[4u3g]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4u3g]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecol6 Ecol6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U3G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U3G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4u3g]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_CFT073 Escherichia coli CFT073]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U3G FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bfr, c4107 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=199310 ECOL6])</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=4u3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u3g OCA], [https://pdbe.org/4u3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u3g RCSB], [https://www.ebi.ac.uk/pdbsum/4u3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u3g ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </span></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=4u3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u3g OCA], [http://pdbe.org/4u3g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u3g RCSB], [http://www.ebi.ac.uk/pdbsum/4u3g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u3g ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BFR_ECOL6 BFR_ECOL6]] 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). | + | [https://www.uniprot.org/uniprot/BFR_ECOL6 BFR_ECOL6] 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). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4u3g" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4u3g" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecol6]] | + | [[Category: Escherichia coli CFT073]] |
| - | [[Category: Ferroxidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Brun, N E.Le]] | + | [[Category: Grigg JC]] |
| - | [[Category: Grigg, J C]] | + | [[Category: Le Brun NE]] |
| - | [[Category: Mauk, A G]] | + | [[Category: Mauk AG]] |
| - | [[Category: Moore, G R]] | + | [[Category: Moore GR]] |
| - | [[Category: Murphy, M E.P]] | + | [[Category: Murphy MEP]] |
| - | [[Category: Wong, S G]] | + | [[Category: Wong SG]] |
| - | [[Category: 4-helix bundle]]
| + | |
| - | [[Category: Diiron site]]
| + | |
| - | [[Category: Iron channel]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
BFR_ECOL6 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).
Publication Abstract from PubMed
Bacterioferritin is a bacterial iron storage and detoxification protein that is capable of forming a ferric oxyhydroxide mineral core within its central cavity. To do this, iron must traverse the bacterioferritin protein shell, which is expected to occur through one or more of the channels through the shell identified by structural studies. The size and negative electrostatic potential of the 24 B-type channels suggest that they could provide a route for iron into bacterioferritin. Residues at the B-type channel (N34, E66, D132, and D139)of E. coli bacterioferritin were substituted to determine if they are important for iron core formation. A significant decrease in the rates of initial oxidation of Fe(II) at the ferroxidase center and subsequent iron mineralization was observed for the D132F variant. The crystal structure of this variant shows that substitution of residue 132 with phenylalanine caused a steric blockage of the B-type channel and no other material structural perturbation. We conclude that the B-type channel is a major route for iron entry into both the ferroxidase center and the iron storage cavity of bacterioferritin.
The B-type Channel is a Major Route for Iron Entry into the Ferroxidase Center and Central Cavity of Bacterioferritin.,Wong SG, Grigg JC, Le Brun NE, Moore GR, Murphy ME, Mauk AG J Biol Chem. 2014 Dec 15. pii: jbc.M114.623082. PMID:25512375[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wong SG, Grigg JC, Le Brun NE, Moore GR, Murphy ME, Mauk AG. The B-type Channel is a Major Route for Iron Entry into the Ferroxidase Center and Central Cavity of Bacterioferritin. J Biol Chem. 2014 Dec 15. pii: jbc.M114.623082. PMID:25512375 doi:http://dx.doi.org/10.1074/jbc.M114.623082
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