4xgs: Difference between revisions
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<StructureSection load='4xgs' size='340' side='right'caption='[[4xgs]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='4xgs' size='340' side='right'caption='[[4xgs]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xgs]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4xgs]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XGS FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OFO:HYDROXY+DIIRON-OXO+MOIETY'>OFO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OFO:HYDROXY+DIIRON-OXO+MOIETY'>OFO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4xgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xgs OCA], [https://pdbe.org/4xgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xgs RCSB], [https://www.ebi.ac.uk/pdbsum/4xgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xgs ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/FTNA_ECOLI FTNA_ECOLI] Iron-storage protein. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kim | [[Category: Kim S]] | ||
Revision as of 12:58, 19 April 2023
Crystal structure analysis of novel iron uptake mechanism of Gram-negative bacterial ferritinCrystal structure analysis of novel iron uptake mechanism of Gram-negative bacterial ferritin
Structural highlights
FunctionFTNA_ECOLI Iron-storage protein. Publication Abstract from PubMedIron and oxygen chemistry is mediated by iron proteins for many biological functions. Carboxylate-bridged diiron enzymes including ferritin have the common mechanism of oxygen activation via peroxodiferric intermediates. However, the route for iron uptake and the structural identification of intermediates still remain incomplete. The 4-fold symmetry channel of Helicobacter pylori ferritin was previously proposed as the iron-uptake route in eubacteria, but the amino acid residues at the 4-fold channel are not highly conserved. Here, we show evidence for a short path for iron uptake from His93 on the surface to the ferroxidase center in H. pylori ferritin and Escherichia coli ferritin. The amino acid residues along this path are highly conserved in Gram-negative bacteria and some archaea, and the mutants containing S20A and H93L showed significantly decreased iron oxidation. Surprisingly, the E. coli ferritin S20A crystal structure showed oxygen binding and side-on, symmetric mu-eta2:eta2 peroxodiferric and oxodiferric intermediates. The results provide the structural basis for understanding the chemical nature of intermediates in iron oxidation in bacteria and some of archaea. Structural Basis of Novel Iron-Uptake Route and Reaction Intermediates in Ferritins from Gram-Negative Bacteria.,Kim S, Lee JH, Seok JH, Park YH, Jung SW, Cho AE, Lee C, Chung MS, Kim KH J Mol Biol. 2016 Dec 4;428(24 Pt B):5007-5018. doi: 10.1016/j.jmb.2016.10.022., Epub 2016 Oct 21. PMID:27777002[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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