5fnn: Difference between revisions
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==Iron and Selenomethionine containing Iron sulfur cluster repair protein YtfE== | ==Iron and Selenomethionine containing Iron sulfur cluster repair protein YtfE== | ||
<StructureSection load='5fnn' size='340' side='right' caption='[[5fnn]], [[Resolution|resolution]] 2.09Å' scene=''> | <StructureSection load='5fnn' size='340' side='right'caption='[[5fnn]], [[Resolution|resolution]] 2.09Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5fnn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FNN OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5fnn]] 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=5FNN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FNN FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</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=5fnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fnn OCA], [https://pdbe.org/5fnn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fnn RCSB], [https://www.ebi.ac.uk/pdbsum/5fnn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fnn 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/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> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Molecular mechanisms underlying the repair of nitrosylated [Fe-S] clusters by the microbial protein YtfE remain poorly understood. The X-ray crystal structure of YtfE, in combination with EPR, magnetic circular dichroism (MCD), UV, and 17 O-labeling electron spin echo envelope modulation measurements, show that each iron of the oxo-bridged FeII -FeIII diiron core is coordinatively unsaturated with each iron bound to two bridging carboxylates and two terminal histidines in addition to an oxo-bridge. Structural analysis reveals that there are two solvent-accessible tunnels, both of which converge to the diiron center and are critical for capturing substrates. The reactivity of the reduced-form FeII -FeII YtfE toward nitric oxide demonstrates that the prerequisite for N2 O production requires the two iron sites to be nitrosylated simultaneously. Specifically, the nitrosylation of the two iron sites prior to their reductive coupling to produce N2 O is cooperative. This result suggests that, in addition to any repair of iron centers (RIC) activity, YtfE acts as an NO-trapping scavenger to promote the NO to N2 O transformation under low NO flux, which precedes nitrosative stress. | |||
Crystal Structure Analysis of the Repair of Iron Centers Protein YtfE and Its Interaction with NO.,Lo FC, Hsieh CC, Maestre-Reyna M, Chen CY, Ko TP, Horng YC, Lai YC, Chiang YW, Chou CM, Chiang CH, Huang WN, Lin YH, Bohle DS, Liaw WF Chemistry. 2016 Jun 1. doi: 10.1002/chem.201600990. PMID:27246459<ref>PMID:27246459</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5fnn" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Chen | [[Category: Escherichia coli K-12]] | ||
[[Category: Chiang | [[Category: Large Structures]] | ||
[[Category: Chiang | [[Category: Chen C-Y]] | ||
[[Category: Chou | [[Category: Chiang C-H]] | ||
[[Category: Horng | [[Category: Chiang Y-W]] | ||
[[Category: Hsieh | [[Category: Chou C-M]] | ||
[[Category: Huang | [[Category: Horng Y-C]] | ||
[[Category: Ko | [[Category: Hsieh C-C]] | ||
[[Category: Lai | [[Category: Huang W-N]] | ||
[[Category: Liaw | [[Category: Ko T-P]] | ||
[[Category: Lo | [[Category: Lai Y-C]] | ||
[[Category: Maestre-Reyna | [[Category: Liaw W-F]] | ||
[[Category: Lo F-C]] | |||
[[Category: Maestre-Reyna M]] | |||
Latest revision as of 06:59, 19 July 2023
Iron and Selenomethionine containing Iron sulfur cluster repair protein YtfE
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