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| | <StructureSection load='4cvp' size='340' side='right'caption='[[4cvp]], [[Resolution|resolution]] 2.11Å' scene=''> | | <StructureSection load='4cvp' size='340' side='right'caption='[[4cvp]], [[Resolution|resolution]] 2.11Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cvp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CVP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CVP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cvp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CVP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CVP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | + | </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></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cvr|4cvr]], [[4cvs|4cvs]], [[4cvt|4cvt]]</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=4cvp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cvp OCA], [https://pdbe.org/4cvp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cvp RCSB], [https://www.ebi.ac.uk/pdbsum/4cvp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cvp 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=4cvp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cvp OCA], [http://pdbe.org/4cvp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cvp RCSB], [http://www.ebi.ac.uk/pdbsum/4cvp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cvp 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_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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ferritin|Ferritin]] | + | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Ferroxidase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cheah, M H]] | + | [[Category: Cheah MH]] |
| - | [[Category: Hillier, W]] | + | [[Category: Hillier W]] |
| - | [[Category: Hingorani, K]] | + | [[Category: Hingorani K]] |
| - | [[Category: Murray, J W]] | + | [[Category: Murray JW]] |
| - | [[Category: Pace, R]] | + | [[Category: Pace R]] |
| - | [[Category: Smith, P]] | + | [[Category: Smith P]] |
| - | [[Category: Whitney, S]] | + | [[Category: Whitney S]] |
| - | [[Category: Wydrzynski, T]] | + | [[Category: Wydrzynski T]] |
| - | [[Category: Electron transfer]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
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]
Publication Abstract from PubMed
The photosynthetic reaction centre (RC) is central to the conversion of solar energy into chemical energy and is a model for bio-mimetic engineering approaches to this end. We describe bio-engineering of a Photosystem II (PSII) RC inspired peptide model, building on our earlier studies. A non-photosynthetic haem containing bacterioferritin (BFR) from Escherichia coli that expresses as a homodimer was used as a protein scaffold, incorporating redox-active cofactors mimicking those of PSII. Desirable properties include: a di-nuclear metal binding site which provides ligands for class II metals, a hydrophobic pocket at the dimer interface which can bind a photosensitive porphyrin and presence of tyrosine residues proximal to the bound cofactors, which can be utilised as efficient electron-tunnelling intermediates. Light-induced electron transfer from proximal tyrosine residues to the photo-oxidised ZnCe6*+, in the modified BFR reconstituted with both ZnCe6 and MnII, is presented. Three site-specific tyrosine variants (Y25F, Y58F and Y45F) were made to localise the redox-active tyrosine in the engineered system. The results indicate that: presence of bound MnII is necessary to observe tyrosine oxidation in all BFR variants; Y45 the most important tyrosine as an immediate electron donor to the oxidised ZnCe6*+; and that Y25 and Y58 are both redox-active in this system, but appear to function interchangebaly. High-resolution (2.1A) crystal structures of the tyrosine variants show that there are no mutation-induced effects on the overall 3-D structure of the protein. Small effects are observed in the Y45F variant. Here, the BFR-RC represents a protein model for artificial photosynthesis.
Photo-oxidation of tyrosine in a bio-engineered bacterioferritin 'reaction centre'-A protein model for artificial photosynthesis.,Hingorani K, Pace R, Whitney S, Murray JW, Smith P, Cheah MH, Wydrzynski T, Hillier W Biochim Biophys Acta. 2014 Aug 5. pii: S0005-2728(14)00557-X. doi:, 10.1016/j.bbabio.2014.07.019. PMID:25107631[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ 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
- ↑ Hingorani K, Pace R, Whitney S, Murray JW, Smith P, Cheah MH, Wydrzynski T, Hillier W. Photo-oxidation of tyrosine in a bio-engineered bacterioferritin 'reaction centre'-A protein model for artificial photosynthesis. Biochim Biophys Acta. 2014 Aug 5. pii: S0005-2728(14)00557-X. doi:, 10.1016/j.bbabio.2014.07.019. PMID:25107631 doi:http://dx.doi.org/10.1016/j.bbabio.2014.07.019
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