4cvt

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m (Protected "4cvt" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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==Structure of Apobacterioferritin Y58F variant==
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<StructureSection load='4cvt' size='340' side='right' caption='[[4cvt]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4cvt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CVT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CVT FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cvp|4cvp]], [[4cvr|4cvr]], [[4cvs|4cvs]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cvt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cvt RCSB], [http://www.ebi.ac.uk/pdbsum/4cvt PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 4cvt is ON HOLD until Paper Publication
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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<ref>PMID:25107631</ref>
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Authors: Hingorani, K., Pace, R., Whitney, S., Murray, J.W., Wydrzynski, T., Cheah, M.H., Smith, P., Hillier, W.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Structure of Apobacterioferritin Y58F variant
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Cheah, M H.]]
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[[Category: Hillier, W.]]
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[[Category: Hingorani, K.]]
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[[Category: Murray, J W.]]
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[[Category: Pace, R.]]
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[[Category: Smith, P.]]
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[[Category: Whitney, S.]]
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[[Category: Wydrzynski, T.]]
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[[Category: Electron transfer]]
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[[Category: Oxidoreductase]]

Revision as of 16:23, 20 August 2014

Structure of Apobacterioferritin Y58F variant

4cvt, resolution 1.79Å

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