1sof

From Proteopedia

(Difference between revisions)

Revision as of 07:34, 22 September 2021

Crystal structure of the azotobacter vinelandii bacterioferritin at 2.6 A resolution

Structural highlights

1sof is a 8 chain structure with sequence from Azotobacter vinelandii. 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_AZOVI] 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 (By similarity).

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 the bacterioferritin from Azotobacter vinelandii has been determined at 2.6 A resolution. Both the low occupancy of one iron ion in the dinuclear iron center and the deviation of its adjacent residue His130 from the center suggest migration of the iron ion from the dinuclear iron site to the inner nucleation site. The concerted movement of His130 and Glu47 may admit a dynamic gating mechanism for shift of the oxidized iron ion. Ba2+ binding to the fourfold channel implicates that the channel bears Fe2+ conductivity and selectivity to provide a route for iron access to the inner cavity during core formation.

2.6 A resolution crystal structure of the bacterioferritin from Azotobacter vinelandii.,Liu HL, Zhou HN, Xing WM, Zhao JF, Li SX, Huang JF, Bi RC FEBS Lett. 2004 Aug 27;573(1-3):93-8. PMID:15327981^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Liu HL, Zhou HN, Xing WM, Zhao JF, Li SX, Huang JF, Bi RC. 2.6 A resolution crystal structure of the bacterioferritin from Azotobacter vinelandii. FEBS Lett. 2004 Aug 27;573(1-3):93-8. PMID:15327981 doi:10.1016/j.febslet.2004.07.054

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/1sof"

@@ Line 3: / Line 3: @@
 <StructureSection load='1sof' size='340' side='right'caption='[[1sof]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1sof]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SOF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1sof]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SOF FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1sof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sof OCA], [http://pdbe.org/1sof PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sof RCSB], [http://www.ebi.ac.uk/pdbsum/1sof PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sof 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=1sof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sof OCA], [https://pdbe.org/1sof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sof RCSB], [https://www.ebi.ac.uk/pdbsum/1sof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sof ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BFR_AZOVI BFR_AZOVI]] 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 (By similarity).
+[[https://www.uniprot.org/uniprot/BFR_AZOVI BFR_AZOVI]] 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 (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1sof

From Proteopedia

Revision as of 07:34, 22 September 2021

Crystal structure of the azotobacter vinelandii bacterioferritin at 2.6 A resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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