2htn

From Proteopedia

(Difference between revisions)

Current revision

E. coli bacterioferritin in its as-isolated form

Structural highlights

2htn is a 8 chain structure with sequence from Escherichia coli BL21. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	,
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

Escherichia coli bacterioferritin was serendipitously crystallized in a novel cubic crystal form and its structure could be determined to 2.5 A resolution despite a high degree of merohedral twinning. This is the first report of crystallographic data on 'as-isolated' E. coli bacterioferritin. The ferroxidase active site contains positive difference density consistent with two metal ions that had co-purified with the protein. X-ray fluorescence studies suggest that the metal composition is different from that of previous structures and is a mix of zinc and native iron ions. The ferroxidase-centre configuration displays a similar flexibility as previously noted for other bacterioferritins.

Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form.,van Eerde A, Wolterink-van Loo S, van der Oost J, Dijkstra BW Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1061-6. Epub 2006 Oct 25. PMID:17077480^[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
↑ van Eerde A, Wolterink-van Loo S, van der Oost J, Dijkstra BW. Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1061-6. Epub 2006 Oct 25. PMID:17077480 doi:10.1107/S1744309106039583

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/2htn"

@@ Line 1: / Line 1: @@
 ==E. coli bacterioferritin in its as-isolated form==
-<StructureSection load='2htn' size='340' side='right' caption='[[2htn]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='2htn' size='340' side='right'caption='[[2htn]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2htn]] is a 8 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=2HTN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HTN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2htn]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21 Escherichia coli BL21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HTN 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>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=2htn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2htn OCA], [http://pdbe.org/2htn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2htn RCSB], [http://www.ebi.ac.uk/pdbsum/2htn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2htn ProSAT]</span></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=2htn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2htn OCA], [https://pdbe.org/2htn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2htn RCSB], [https://www.ebi.ac.uk/pdbsum/2htn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2htn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Ferritin|Ferritin]]
+*[[Ferritin 3D structures|Ferritin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Escherichia coli BL21]]
-[[Category: Ferroxidase]]
+[[Category: Large Structures]]
-[[Category: Dijkstra, B W]]
+[[Category: Dijkstra BW]]
-[[Category: Eerde, A van]]
+[[Category: Van Der Oost J]]
-[[Category: Loo, S Wolterink-Van]]
+[[Category: Wolterink-Van Loo S]]
-[[Category: Oost, J Van Der]]
+[[Category: Van Eerde A]]
-[[Category: Ferroxidase centre]]
-[[Category: Four-helix bundle]]
-[[Category: Haem]]
-[[Category: Iron binding site]]
-[[Category: Metal binding protein]]
-[[Category: Oxidoreductase]]
-[[Category: Protein shell]]

2htn

From Proteopedia

Current revision

E. coli bacterioferritin in its as-isolated form

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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