3egm: Difference between revisions

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 <StructureSection load='3egm' size='340' side='right'caption='[[3egm]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3egm]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_pylori_j99 Campylobacter pylori j99]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EGM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3egm]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_J99 Helicobacter pylori J99]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EGM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 2.1&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftnA, pfr, jhp_0598 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85963 Campylobacter pylori J99])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3egm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3egm OCA], [https://pdbe.org/3egm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3egm RCSB], [https://www.ebi.ac.uk/pdbsum/3egm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3egm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/FTN_HELPJ FTN_HELPJ]] Iron-storage protein (By similarity).
+[https://www.uniprot.org/uniprot/FTN_HELPJ FTN_HELPJ] Iron-storage protein (By similarity).
 == 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=3egm ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The crystal structure of recombinant ferritin from Helicobacter pylori has been determined in its apo, low-iron-bound, intermediate, and high-iron-bound states. Similar to other members of the ferritin family, the bacterial ferritin assembles as a spherical protein shell of 24 subunits, each of which folds into a four-alpha-helix bundle. Significant conformational changes were observed at the BC loop and the entrance of the 4-fold symmetry channel in the intermediate and high-iron-bound states, whereas no change was found in the apo and low-iron-bound states. The imidazole rings of His149 at the channel entrance undergo conformational changes that bear resemblance to heme configuration and are directly coupled to axial translocation of Fe ions through the 4-fold channel. Our results provide the first structural evidence of the translocation of Fe ions through the 4-fold channel in prokaryotes and the transition from a protein-dominated process to a mineral-surface-dominated process during biomineralization.
-The crystal structure of ferritin from Helicobacter pylori reveals unusual conformational changes for iron uptake.,Cho KJ, Shin HJ, Lee JH, Kim KJ, Park SS, Lee Y, Lee C, Park SS, Kim KH J Mol Biol. 2009 Jul 3;390(1):83-98. Epub 2009 May 7. PMID:19427319<ref>PMID:19427319</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3egm" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Ferritin 3D structures|Ferritin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Campylobacter pylori j99]]
+[[Category: Helicobacter pylori J99]]
-[[Category: Ferroxidase]]
 [[Category: Large Structures]]
-[[Category: Cho, K J]]
+[[Category: Cho KJ]]
-[[Category: Kim, K H]]
+[[Category: Kim KH]]
-[[Category: Lee, J H]]
+[[Category: Lee JH]]
-[[Category: Shin, H J]]
+[[Category: Shin HJ]]
-[[Category: Iron]]
-[[Category: Iron storage]]
-[[Category: Metal-binding]]
-[[Category: Oxidoreductase]]