5d8s: Difference between revisions
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<StructureSection load='5d8s' size='340' side='right'caption='[[5d8s]], [[Resolution|resolution]] 2.55Å' scene=''> | <StructureSection load='5d8s' size='340' side='right'caption='[[5d8s]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5d8s]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5d8s]] is a 12 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=5D8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D8S FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=5d8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d8s OCA], [https://pdbe.org/5d8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d8s RCSB], [https://www.ebi.ac.uk/pdbsum/5d8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d8s 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/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] | ||
<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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas aeruginosa PAO1]] | ||
[[Category: Battaile | [[Category: Battaile KP]] | ||
[[Category: Lovell | [[Category: Lovell S]] | ||
[[Category: Rivera | [[Category: Rivera M]] | ||
[[Category: Wang | [[Category: Wang Y]] | ||
[[Category: Yao | [[Category: Yao H]] | ||
Revision as of 13:26, 21 June 2023
2.55A resolution structure of BfrB (E85A) from Pseudomonas aeruginosa2.55A resolution structure of BfrB (E85A) from Pseudomonas aeruginosa
Structural highlights
FunctionQ9HY79_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] Publication Abstract from PubMedMobilization of iron stored in the interior cavity of BfrB requires electron transfer from the [2Fe-2S] cluster in Bfd to the core iron in BfrB. A crystal structure of the P. aeruginosa BfrB:Bfd complex revealed that BfrB can bind up to 12 Bfd molecules at 12 structurally identical binding sites, placing the [2Fe-2S] cluster of each Bfd immediately above a heme group in BfrB [Yao, H., Wang, Y., Lovell, S., Kumar, R., Ruvinsky, A. M., Battaile, K. P., Vakser, I. A., and Rivera, M. J. Am. Chem. Soc. (2012), 134, 13470-13481]. We report here a study aimed at characterizing the strength of the P. aeruginosa BfrB:Bfd association using surface plasmon resonance and isothermal titration calorimetry, as well as determining the binding energy hot spots at the protein-protein interaction interface. The results show that the 12 Bfd-binding sites on BfrB are equivalent and independent, and that the protein-protein association at each of these sites is driven entropically and is characterized by a dissociation constant (Kd) of approximately 3 muM. Determination of the binding energy hot spots was carried out by replacing certain residues that comprise the protein-protein interface with alanine, and by evaluating the effect of the mutation on Kd and on the efficiency of core iron mobilization from BfrB. The results identified hot-spot residues in both proteins [L_B^68, E_A^81 and E_A^85 in BfrB (superscript for residue number and subscript for chain) and Y2 and L5 in Bfd], which network at the interface to produce a highly complementary hot region for the interaction. The hot-spot residues are conserved in the amino acid sequences of Bfr and Bfd proteins from a number of gram negative pathogens, indicating that the BfrB:Bfd interaction is of widespread significance in bacterial iron metabolism. Characterization of the Bacterioferritin/Bacterioferritin Associated Ferredoxin (BfrB:Bfd) Protein-Protein Interaction in Solution and Determination of Binding Energy Hot Spots.,Wang Y, Yao H, Cheng Y, Lovell SW, Battaile KP, Middaugh CR, Rivera M Biochemistry. 2015 Sep 28. PMID:26368531[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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