This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1bfr

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:58, 8 November 2017

IRON STORAGE AND ELECTRON TRANSPORT

Structural highlights

1bfr is a 24 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:	,
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

Crystals of E. coli cytochrome b1, alias bacterioferritin, were grown fr om a low ionic strength solution. The resulting monoclniic P21 structure was solved by molecular replacement and refined using noncrystallographi c symmetries applied to the fundamental unit, consisting of two protein subunits and a single haem. From the Patterson self-rotation results it was shown that the asymmetric unit of the monoclinic crystal consists of 12 such dimers and corresponds to a complete, nearly spherical, molecule of bacterioferritin (M4 = 450 kDa) of 432 point-group symmetry. It is thus the most symmetrical cytochrome. As previously determined for the tetragonal form, the haem is located in a special position on a local twofold axis of the dimer. A bimetal centre is also observed within the four-helix bundle of each monomer; a metal-binding site is located on the fourfold axis.

Structure of a monoclinic crystal from of cyctochrome b1 (Bacterioferritin) from E. coli.,Dautant A, Meyer JB, Yariv J, Precigoux G, Sweet RM, Kalb AJ, Frolow F Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):16-24. PMID:9867433^[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
↑ Dautant A, Meyer JB, Yariv J, Precigoux G, Sweet RM, Kalb AJ, Frolow F. Structure of a monoclinic crystal from of cyctochrome b1 (Bacterioferritin) from E. coli. Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):16-24. PMID:9867433

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bfr"

@@ Line 1: / Line 1: @@
 ==IRON STORAGE AND ELECTRON TRANSPORT==
 <StructureSection load='1bfr' size='340' side='right' caption='[[1bfr]], [[Resolution|resolution]] 2.94&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1bfr]] is a 24 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=1BFR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BFR 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=MN:MANGANESE+(II)+ION'>MN</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=1bfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfr OCA], [http://pdbe.org/1bfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bfr RCSB], [http://www.ebi.ac.uk/pdbsum/1bfr 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=1bfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfr OCA], [http://pdbe.org/1bfr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bfr RCSB], [http://www.ebi.ac.uk/pdbsum/1bfr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bfr ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 1bfr" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Ferritin|Ferritin]]
 == References ==
 <references/>

1bfr

From Proteopedia

Revision as of 10:58, 8 November 2017

IRON STORAGE AND ELECTRON TRANSPORT

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox