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5d8x

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1.50A resolution structure of BfrB (L68A E81A) from Pseudomonas aeruginosa

Structural highlights

5d8x is a 24 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.5Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wang Y, Yao H, Cheng Y, Lovell SW, Battaile KP, Middaugh CR, Rivera M. Characterization of the Bacterioferritin/Bacterioferritin Associated Ferredoxin (BfrB:Bfd) Protein-Protein Interaction in Solution and Determination of Binding Energy Hot Spots. Biochemistry. 2015 Sep 28. PMID:26368531 doi:http://dx.doi.org/10.1021/acs.biochem.5b00937

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5d8x"

@@ Line 1: / Line 1: @@
 ==1.50A resolution structure of BfrB (L68A E81A) from Pseudomonas aeruginosa==
-<StructureSection load='5d8x' size='340' side='right' caption='[[5d8x]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+<StructureSection load='5d8x' size='340' side='right'caption='[[5d8x]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5d8x]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D8X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D8X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5d8x]] is a 24 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=5D8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D8X 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>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d8o|5d8o]], [[5d8p|5d8p]], [[5d8q|5d8q]], [[5d8r|5d8r]], [[5d8s|5d8s]], [[5d8y|5d8y]]</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>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </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=5d8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d8x OCA], [https://pdbe.org/5d8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d8x RCSB], [https://www.ebi.ac.uk/pdbsum/5d8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d8x ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d8x OCA], [http://pdbe.org/5d8x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d8x RCSB], [http://www.ebi.ac.uk/pdbsum/5d8x PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://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]
+[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 ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5d8x" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ferritin 3D structures|Ferritin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Ferroxidase]]
+[[Category: Large Structures]]
-[[Category: Battaile, K P]]
+[[Category: Pseudomonas aeruginosa PAO1]]
-[[Category: Lovell, S]]
+[[Category: Battaile KP]]
-[[Category: Rivera, M]]
+[[Category: Lovell S]]
-[[Category: Wang, Y]]
+[[Category: Rivera M]]
-[[Category: Yao, H]]
+[[Category: Wang Y]]
-[[Category: Electron transport]]
+[[Category: Yao H]]
-[[Category: Iron binding]]
-[[Category: Iron mobilization]]
-[[Category: Iron storage]]
-[[Category: Oxidoreductase]]

5d8x

From Proteopedia

Current revision

1.50A resolution structure of BfrB (L68A E81A) from Pseudomonas aeruginosa

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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