4toe: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4toe]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TOE FirstGlance]. <br>
<table><tr><td colspan='2'>[[4toe]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TOE FirstGlance]. <br>
</td></tr><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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.2&#8491;</td></tr>
<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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=4toe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4toe OCA], [https://pdbe.org/4toe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4toe RCSB], [https://www.ebi.ac.uk/pdbsum/4toe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4toe ProSAT]</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=4toe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4toe OCA], [https://pdbe.org/4toe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4toe RCSB], [https://www.ebi.ac.uk/pdbsum/4toe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4toe ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q9HY79_PSEAE Q9HY79_PSEAE] Iron-storage protein (By similarity). 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 (By similarity).[PIRNR:PIRNR002560]
[https://www.uniprot.org/uniprot/BFRB_PSEAE BFRB_PSEAE] The major iron-storage protein, part of the heterooligomeric bacterioferritin (BFR) complex. The ferroxidase center binds Fe(2+), oxidizes it using dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the BFR protein shell. Can store up to 600 iron atoms per bacterioferritin protein molecule (PubMed:19575528, PubMed:20067302, PubMed:25640193, PubMed:26368531). In iron-sufficient conditions (10 uM Fe(2+)) iron accumulates in BFR until about 12 hours, when it starts to deplete; stored iron is no longer detectable by 24 hours growth, iron is mobilized from the BFR as levels drop in the growth media (PubMed:28318006). Iron release from the BFR requires ferredoxin NADP reductase (FPR) and bacterioferritin-associated ferredoxin (Bfd) (PubMed:19575528, PubMed:22812654, PubMed:26368531). Reduction of the BfrB heme group occurs in the presence of Bfd, strongly suggesting that the BfrB-Bfd complex allows heme to mediate electron transfer from FPR to the Fe(3+) iron core in the BFR shell prior to its release as Fe(2+) (PubMed:19575528, PubMed:22812654, PubMed:26368531).<ref>PMID:19575528</ref> <ref>PMID:20067302</ref> <ref>PMID:22812654</ref> <ref>PMID:25640193</ref> <ref>PMID:26368531</ref> <ref>PMID:28318006</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==