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2vxi

From Proteopedia

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Revision as of 08:41, 25 June 2020

The binding of heme and zinc in Escherichia coli Bacterioferritin

Structural highlights

2vxi is a 12 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1bfr, 1bcf, 2htn
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.

Publication Abstract from PubMed

The 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.

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
↑ Willies SC, Isupov MN, Garman EF, Littlechild JA. The binding of haem and zinc in the 1.9 A X-ray structure of Escherichia coli bacterioferritin. J Biol Inorg Chem. 2008 Oct 23. PMID:18946693 doi:10.1007/s00775-008-0438-8

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vxi"

@@ Line 1: / Line 1: @@
 ==The binding of heme and zinc in Escherichia coli Bacterioferritin==
-<StructureSection load='2vxi' size='340' side='right' caption='[[2vxi]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
+<StructureSection load='2vxi' size='340' side='right'caption='[[2vxi]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vxi]] is a 12 chain structure 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=2VXI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VXI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vxi]] is a 12 chain structure 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=2VXI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VXI FirstGlance]. <br>
-</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" id="ligandDat"><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='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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
 == Function ==
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Ferritin|Ferritin]]
+*[[Ferritin 3D structures|Ferritin 3D structures]]
 == References ==
 <references/>
@@ Line 37: / Line 37: @@
 </StructureSection>
 [[Category: Escherichia coli]]
+[[Category: Large Structures]]
 [[Category: Garman, E F]]
 [[Category: Isupov, M N]]

2vxi

From Proteopedia

Revision as of 08:41, 25 June 2020

The binding of heme and zinc in Escherichia coli Bacterioferritin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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