3ka6: Difference between revisions

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-[[Image:3ka6.png|left|200px]]
+==Frog M-ferritin, EED mutant, with cobalt==
+<StructureSection load='3ka6' size='340' side='right' caption='[[3ka6]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3ka6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rana_catesbeiana Rana catesbeiana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KA6 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ka3|3ka3]], [[3ka4|3ka4]], [[3ka8|3ka8]], [[3ka9|3ka9]]</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='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=3ka6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ka6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ka6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ka6 PDBsum]</span></td></tr>
+</table>
+== 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/ka/3ka6_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/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Ferritin nanocages synthesize ferric oxide minerals, containing hundreds to thousands of Fe(III) diferric oxo/hydroxo complexes, by reactions of Fe(II) ions with O(2) at multiple di-iron catalytic centers. Ferric-oxy multimers, tetramers, and/or larger mineral nuclei form during postcatalytic transit through the protein cage, and mineral accretion occurs in the central cavity. We determined how Fe(II) substrates can access catalytic sites using frog M ferritins, active and inactivated by ligand substitution, crystallized with 2.0 M Mg(II) +/- 0.1 M Co(II) for Co(II)-selective sites. Co(II) inhibited Fe(II) oxidation. High-resolution (&lt;1.5 A) crystal structures show (1) a line of metal ions, 15 A long, which penetrates the cage and defines ion channels and internal pores to the nanocavity that link external pores to the cage interior, (2) metal ions near negatively charged residues at the channel exits and along the inner cavity surface that model Fe(II) transit to active sites, and (3) alternate side-chain conformations, absent in ferritins with catalysis eliminated by amino acid substitution, which support current models of protein dynamics and explain changes in Fe-Fe distances observed during catalysis. The new structural data identify a approximately 27-A path Fe(II) ions can follow through ferritin entry channels between external pores and the central cavity and along the cavity surface to the active sites where mineral synthesis begins. This "bucket brigade" for Fe(II) ion access to the ferritin catalytic sites not only increases understanding of biological nanomineral synthesis but also reveals unexpected design principles for protein cage-based catalysts and nanomaterials.
-{{STRUCTURE_3ka6|  PDB=3ka6  |  SCENE=  }}
+Moving metal ions through ferritin-protein nanocages from three-fold pores to catalytic sites.,Tosha T, Ng HL, Bhattasali O, Alber T, Theil EC J Am Chem Soc. 2010 Oct 20;132(41):14562-9. PMID:20866049<ref>PMID:20866049</ref>
-===Frog M-ferritin, EED mutant, with cobalt===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_20866049}}
-==About this Structure==
-[[3ka6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rana_catesbeiana Rana catesbeiana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KA6 OCA].
 ==See Also==
 *[[Ferritin|Ferritin]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:020866049</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Ferroxidase]]
 [[Category: Rana catesbeiana]]
-[[Category: Alber, T.]]
+[[Category: Alber, T]]
-[[Category: Bhattasali, O.]]
+[[Category: Bhattasali, O]]
-[[Category: Ng, H L.]]
+[[Category: Ng, H L]]
-[[Category: Theil, E.]]
+[[Category: Theil, E]]
-[[Category: Tosha, T.]]
+[[Category: Tosha, T]]
 [[Category: Diiron]]
 [[Category: Iron]]