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7be8

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<StructureSection load='7be8' size='340' side='right'caption='[[7be8]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
<StructureSection load='7be8' size='340' side='right'caption='[[7be8]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7be8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BE8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7be8]] is a 2 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=7BE8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BE8 FirstGlance]. <br>
</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=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</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=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</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=7be8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7be8 OCA], [https://pdbe.org/7be8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7be8 RCSB], [https://www.ebi.ac.uk/pdbsum/7be8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7be8 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=7be8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7be8 OCA], [https://pdbe.org/7be8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7be8 RCSB], [https://www.ebi.ac.uk/pdbsum/7be8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7be8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/YTFE_ECOLI YTFE_ECOLI]] Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions.<ref>PMID:16553864</ref> <ref>PMID:17289666</ref> <ref>PMID:18357473</ref>
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[[https://www.uniprot.org/uniprot/YTFE_ECOLI YTFE_ECOLI]] Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions.<ref>PMID:16553864</ref> <ref>PMID:17289666</ref> <ref>PMID:18357473</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Repair of Iron Center proteins (RIC) form a family of di-iron proteins that are widely spread in the microbial world. RICs contain a binuclear nonheme iron site in a four-helix bundle fold, two basic features of hemerythrin-like proteins. In this work, we review the data on microbial RICs including how their genes are regulated and contribute to the survival of pathogenic bacteria. We gathered the currently available biochemical, spectroscopic and structural data on RICs with a particular focus on Escherichia coli RIC (also known as YtfE), which remains the best-studied protein with extensive biochemical characterization. Additionally, we present novel structural data for Escherichia coli YtfE harboring a di-manganese site and the protein's affinity for this metal. The networking of protein interactions involving YtfE is also described and integrated into the proposed physiological role as an iron donor for reassembling of stress-damaged iron-sulfur centers.
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Repair of Iron Center Proteins-A Different Class of Hemerythrin-like Proteins.,Silva LSO, Matias PM, Romao CV, Saraiva LM Molecules. 2022 Jun 23;27(13). pii: molecules27134051. doi:, 10.3390/molecules27134051. PMID:35807291<ref>PMID:35807291</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7be8" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Matias, P M]]
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[[Category: Matias PM]]
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[[Category: Romao, C V]]
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[[Category: Romao CV]]
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[[Category: Saraiva, L M]]
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[[Category: Saraiva LM]]
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[[Category: Silva, L S.O]]
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[[Category: Silva LSO]]
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[[Category: Di-iron]]
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[[Category: Metal binding protein]]
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Revision as of 05:21, 8 September 2022

Escherichia coli YtfE (Mn)

PDB ID 7be8

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