6e6q: Difference between revisions
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<StructureSection load='6e6q' size='340' side='right'caption='[[6e6q]], [[Resolution|resolution]] 1.20Å' scene=''> | <StructureSection load='6e6q' size='340' side='right'caption='[[6e6q]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6e6q]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6e6q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E6Q FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6e6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e6q OCA], [https://pdbe.org/6e6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e6q RCSB], [https://www.ebi.ac.uk/pdbsum/6e6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e6q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9HY80_PSEAE Q9HY80_PSEAE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Battaile | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Lovell | [[Category: Battaile KP]] | ||
[[Category: Rivera | [[Category: Lovell S]] | ||
[[Category: Wang | [[Category: Rivera M]] | ||
[[Category: Wijerathne | [[Category: Wang Y]] | ||
[[Category: Yao | [[Category: Wijerathne H]] | ||
[[Category: Yao H]] | |||
Latest revision as of 09:20, 11 October 2023
1.20 A resolution structure of the C-terminally truncated [2Fe-2S] ferredoxin (Bfd) from Pseudomonas aeruginosa1.20 A resolution structure of the C-terminally truncated [2Fe-2S] ferredoxin (Bfd) from Pseudomonas aeruginosa
Structural highlights
FunctionPublication Abstract from PubMedMobilization of iron from bacterioferritin (BfrB) requires specific interactions with a [2Fe-2S] ferredoxin (Bfd). Blocking the BfrB:Bfd interaction results in irreversible iron accumulation in BfrB and iron deficiency in the cytosol [Eshelman, K., et al. (2017) Metallomics 9, 646-659]. The only known Bfd structure, which was obtained in complex with BfrB (Protein Data Bank entry 4E6K ), indicated a new fold and suggested that the stability of Bfd is aided by an anion binding site consisting of R26, R29, and K46. We investigated the Bfd fold using site-directed mutagenesis, X-ray crystallography, and biochemistry in solution. The X-ray structure, which is nearly identical to that of Bfd in the BfrB:Bfd complex, shows that the [2Fe-2S] cluster preorganizes residues at the BfrB:Bfd interface into a structure complementary to the Bfd binding site on BfrB. Studies in solution showed rapid loss of the [2Fe-2S] cluster at a low ionic strength but higher stability with an increasing ionic strength, thus supporting a structural anion binding site. Structures of the R26E and R26E/K46Y mutants are nearly identical to that of Bfd, except for a new network of hydrogen bonds stabilizing the region encompassing the former anion binding site. The stability of the R26E and R26E/K46Y mutants, which is weakly and completely independent of solution ionic strength, respectively, corroborates that Bfd requires an anion binding site. The mutations, which caused only small changes to the strength of the BfrB:Bfd interaction and mobilization of iron from BfrB, indicate that the anion binding site in Bfd serves primarily a structural role. Bfd, a New Class of [2Fe-2S] Protein That Functions in Bacterial Iron Homeostasis, Requires a Structural Anion Binding Site.,Wijerathne H, Yao H, Wang Y, Lovell S, Battaile KP, Rivera M Biochemistry. 2018 Sep 13. doi: 10.1021/acs.biochem.8b00823. PMID:30183257[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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