1eum: Difference between revisions

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 <StructureSection load='1eum' size='340' side='right'caption='[[1eum]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1eum]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EUM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1eum]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EUM FirstGlance]. <br>
-</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=1eum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eum OCA], [https://pdbe.org/1eum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eum RCSB], [https://www.ebi.ac.uk/pdbsum/1eum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eum ProSAT]</span></td></tr>
+</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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eum OCA], [https://pdbe.org/1eum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eum RCSB], [https://www.ebi.ac.uk/pdbsum/1eum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eum ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/FTNA_ECOLI FTNA_ECOLI]] Iron-storage protein.
+[https://www.uniprot.org/uniprot/FTNA_ECOLI FTNA_ECOLI] Iron-storage protein.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1eum ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The high-resolution structure of the non-haem ferritin from Escherichia coli (EcFtnA) is presented together with those of its Fe(3+) and Zn(2+) derivatives, this being the first high-resolution X-ray analysis of the iron centres in any ferritin.The binding of both metals is accompanied by small changes in the amino acid ligand positions. Mean Fe(A)(3+)-Fe(B)(3+) and Zn(A)(2+)-Zn(B)(2+) distances are 3.24 A and 3.43 A, respectively. In both derivatives, metal ions at sites A and B are bridged by a glutamate side-chain (Glu50) in a syn-syn conformation. The Fe(3+) derivative alone shows a third metal site (Fe( C)( 3+)) joined to Fe(B)(3+) by a long anti-anti bidentate bridge through Glu130 (mean Fe(B)(3+)-Fe(C)(3+) distance 5.79 A). The third metal site is unique to the non-haem bacterial ferritins.The dinuclear site lies at the inner end of a hydrophobic channel connecting it to the outside surface of the protein shell, which may provide access for dioxygen and possibly for metal ions shielded by water. Models representing the possible binding mode of dioxygen to the dinuclear Fe(3+) pair suggest that a gauche micro-1,2 mode may be preferred stereochemically.Like those of other ferritins, the 24 subunits of EcFtnA are folded as four-helix bundles that assemble into hollow shells and both metals bind at dinuclear centres in the middle of the bundles. The structural similarity of EcFtnA to the human H chain ferritin (HuHF) is remarkable (r.m.s. deviation of main-chain atoms 0.66 A) given the low amino acid sequence identity (22 %). Many of the conserved residues are clustered at the dinuclear centre but there is very little conservation of residues making inter-subunit interactions.
-The high-resolution X-ray crystallographic structure of the ferritin (EcFtnA) of Escherichia coli; comparison with human H ferritin (HuHF) and the structures of the Fe(3+) and Zn(2+) derivatives.,Stillman TJ, Hempstead PD, Artymiuk PJ, Andrews SC, Hudson AJ, Treffry A, Guest JR, Harrison PM J Mol Biol. 2001 Mar 23;307(2):587-603. PMID:11254384<ref>PMID:11254384</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1eum" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Ferritin 3D structures|Ferritin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Andrews, S C]]
+[[Category: Andrews SC]]
-[[Category: Artymiuk, P J]]
+[[Category: Artymiuk PJ]]
-[[Category: Guest, J R]]
+[[Category: Guest JR]]
-[[Category: Harrison, P M]]
+[[Category: Harrison PM]]
-[[Category: Hempstead, P D]]
+[[Category: Hempstead PD]]
-[[Category: Hudson, A J]]
+[[Category: Hudson AJ]]
-[[Category: Stillman, T J]]
+[[Category: Stillman TJ]]
-[[Category: Treffry, A]]
+[[Category: Treffry A]]
-[[Category: E coli non heme ferritin]]
-[[Category: Ecftna]]
-[[Category: Metal binding protein]]