5d8p
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5d8p is ON HOLD until Paper Publication Authors: Lovell, S., Battaile, K.P., Wang, Y., Yao, H., Rivera, M. Description: 2.35A resolution structure ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==2.35A resolution structure of iron bound BfrB (wild-type, C2221 form) from Pseudomonas aeruginosa== | |
| + | <StructureSection load='5d8p' size='340' side='right'caption='[[5d8p]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5d8p]] 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=5D8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D8P FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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></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=5d8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d8p OCA], [https://pdbe.org/5d8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d8p RCSB], [https://www.ebi.ac.uk/pdbsum/5d8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d8p ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mobilization 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<ref>PMID:26368531</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[ | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5d8p" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: Battaile | + | ==See Also== |
| - | [[Category: Lovell | + | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| - | [[Category: Yao | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas aeruginosa PAO1]] | ||
| + | [[Category: Battaile KP]] | ||
| + | [[Category: Lovell S]] | ||
| + | [[Category: Rivera M]] | ||
| + | [[Category: Wang Y]] | ||
| + | [[Category: Yao H]] | ||
Current revision
2.35A resolution structure of iron bound BfrB (wild-type, C2221 form) from Pseudomonas aeruginosa
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