1sof
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1sof" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sof, resolution 2.60Å" /> '''Crystal structure of...) |
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| - | [[Image:1sof.gif|left|200px]]<br /><applet load="1sof" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1sof, resolution 2.60Å" /> | ||
| - | '''Crystal structure of the azotobacter vinelandii bacterioferritin at 2.6 A resolution'''<br /> | ||
| - | == | + | ==Crystal structure of the azotobacter vinelandii bacterioferritin at 2.6 A resolution== |
| - | The crystal structure of the bacterioferritin from Azotobacter vinelandii | + | <StructureSection load='1sof' size='340' side='right'caption='[[1sof]], [[Resolution|resolution]] 2.60Å' scene=''> |
| + | == Structural highlights == | ||
| + | <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</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'>[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 == | ||
| + | [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]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/so/1sof_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </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/main_output.php?pdb_ID=1sof ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:15327981</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1sof" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Ferritin 3D structures|Ferritin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Azotobacter vinelandii]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bi RC]] | ||
| + | [[Category: Huang JF]] | ||
| + | [[Category: Liu HL]] | ||
Current revision
Crystal structure of the azotobacter vinelandii bacterioferritin at 2.6 A resolution
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