2vxi: Difference between revisions
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==THE BINDING OF HEME AND ZINC IN ESCHERICHIA COLI BACTERIOFERRITIN== | ==THE BINDING OF HEME AND ZINC IN ESCHERICHIA COLI BACTERIOFERRITIN== | ||
<StructureSection load='2vxi' size='340' side='right' caption='[[2vxi]], [[Resolution|resolution]] 1.91Å' scene=''> | <StructureSection load='2vxi' size='340' side='right' caption='[[2vxi]], [[Resolution|resolution]] 1.91Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bfr|1bfr]], [[1bcf|1bcf]], [[2htn|2htn]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bfr|1bfr]], [[1bcf|1bcf]], [[2htn|2htn]]</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=2vxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vxi RCSB], [http://www.ebi.ac.uk/pdbsum/2vxi PDBsum]</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=2vxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxi OCA], [http://pdbe.org/2vxi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vxi RCSB], [http://www.ebi.ac.uk/pdbsum/2vxi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vxi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=2vxi ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2vxi" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 22:16, 5 August 2016
THE BINDING OF HEME AND ZINC IN ESCHERICHIA COLI BACTERIOFERRITINTHE BINDING OF HEME AND ZINC IN ESCHERICHIA COLI BACTERIOFERRITIN
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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of Escherichia coli bacterioferritin has been solved to 1.9 A, and shows the symmetrical binding of a haem molecule on the local twofold axis between subunits and a pair of metal atoms bound to each subunit at the ferroxidase centre. These metals have been identified as zinc by the analysis of the structure and X-ray data and confirmed by microfocused proton-induced X-ray emission experiments. For the first time the haem has been shown to be linked to both the internal and the external environments via a cluster of waters positioned above the haem molecule. The binding of haem and zinc in the 1.9 A X-ray structure of Escherichia coli bacterioferritin.,Willies SC, Isupov MN, Garman EF, Littlechild JA J Biol Inorg Chem. 2008 Oct 23. PMID:18946693[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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