1nf4: Difference between revisions

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{{Seed}}
[[Image:1nf4.png|left|200px]]


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==X-Ray Structure of the Desulfovibrio desulfuricans bacterioferritin: the diiron site in different states (reduced structure)==
The line below this paragraph, containing "STRUCTURE_1nf4", creates the "Structure Box" on the page.
<StructureSection load='1nf4' size='340' side='right'caption='[[1nf4]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1nf4]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NF4 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FEC:1,3,5,8-TETRAMETHYL-PORPHINE-2,4,6,7-TETRAPROPIONIC+ACID+FERROUS+COMPLEX'>FEC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_1nf4|  PDB=1nf4  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nf4 OCA], [https://pdbe.org/1nf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nf4 RCSB], [https://www.ebi.ac.uk/pdbsum/1nf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nf4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BFR_DESDA BFR_DESDA] 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.
== 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/nf/1nf4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1nf4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The first crystal structure of a native di-iron center in an iron-storage protein (bacterio)ferritin is reported. The protein, isolated from the anaerobic bacterium Desulfovibrio desulfuricans, has the unique property of having Fe-coproporphyrin III as its heme cofactor. The three-dimensional structure of this bacterioferritin was determined in three distinct catalytic/redox states by X-ray crystallography (at 1.95, 2.05 and 2.35 A resolution), corresponding to different intermediates of the di-iron ferroxidase site. Conformational changes associated with these intermediates support the idea of a route for iron entry into the protein shell through a pore that passes through the di-iron center. Molecular surface and electrostatic potential calculations also suggest the presence of another ion channel, distant from the channels at the three- and four-fold axes proposed as points of entry for the iron atoms.


===X-Ray Structure of the Desulfovibrio desulfuricans bacterioferritin: the diiron site in different states (reduced structure)===
The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans.,Macedo S, Romao CV, Mitchell E, Matias PM, Liu MY, Xavier AV, LeGall J, Teixeira M, Lindley P, Carrondo MA Nat Struct Biol. 2003 Apr;10(4):285-90. PMID:12627224<ref>PMID:12627224</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1nf4" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_12627224}}, adds the Publication Abstract to the page
*[[Ferritin 3D structures|Ferritin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 12627224 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_12627224}}
__TOC__
 
</StructureSection>
==About this Structure==
1NF4 is a 16 chains structure of sequences from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NF4 OCA].
 
==Reference==
<ref group="xtra">PMID:12627224</ref><references group="xtra"/>
[[Category: Desulfovibrio desulfuricans]]
[[Category: Desulfovibrio desulfuricans]]
[[Category: Carrondo, M A.]]
[[Category: Large Structures]]
[[Category: LeGall, J.]]
[[Category: Carrondo MA]]
[[Category: Lindley, P.]]
[[Category: LeGall J]]
[[Category: Liu, M Y.]]
[[Category: Lindley P]]
[[Category: Macedo, S.]]
[[Category: Liu MY]]
[[Category: Matias, P M.]]
[[Category: Macedo S]]
[[Category: Mitchell, E.]]
[[Category: Matias PM]]
[[Category: Romao, C V.]]
[[Category: Mitchell E]]
[[Category: Teixeira, M.]]
[[Category: Romao CV]]
[[Category: Xavier, A V.]]
[[Category: Teixeira M]]
[[Category: Active as 24-mer]]
[[Category: Xavier AV]]
[[Category: Bacterioferritin]]
[[Category: Diiron centre]]
[[Category: Fe-coproporphyrin iii haem cofactor]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:30:45 2009''