7k5e: Difference between revisions

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<StructureSection load='7k5e' size='340' side='right'caption='[[7k5e]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='7k5e' size='340' side='right'caption='[[7k5e]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7k5e]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K5E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7K5E FirstGlance]. <br>
<table><tr><td colspan='2'>[[7k5e]] 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=7K5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K5E FirstGlance]. <br>
</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=VXM:4-{[(5-fluoro-2-hydroxyphenyl)methyl]amino}-1H-isoindole-1,3(2H)-dione'>VXM</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]] 1.75&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bfrB, PA3531 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=VXM:4-{[(5-fluoro-2-hydroxyphenyl)methyl]amino}-1H-isoindole-1,3(2H)-dione'>VXM</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=7k5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k5e OCA], [https://pdbe.org/7k5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k5e RCSB], [https://www.ebi.ac.uk/pdbsum/7k5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k5e ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7k5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k5e OCA], [http://pdbe.org/7k5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7k5e RCSB], [http://www.ebi.ac.uk/pdbsum/7k5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7k5e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 7k5e" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 7k5e" style="background-color:#fffaf0;"></div>
==See Also==
*[[Ferritin 3D structures|Ferritin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ferroxidase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pseae]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Annor-Gyamfi, J K]]
[[Category: Annor-Gyamfi JK]]
[[Category: Battaile, K P]]
[[Category: Battaile KP]]
[[Category: Bunce, R A]]
[[Category: Bunce RA]]
[[Category: Lovell, S]]
[[Category: Lovell S]]
[[Category: Meraz, K]]
[[Category: Meraz K]]
[[Category: Punchi-Hewage, A]]
[[Category: Punchi-Hewage A]]
[[Category: Rivera, M]]
[[Category: Rivera M]]
[[Category: Soldano, A]]
[[Category: Soldano A]]
[[Category: Yao, H]]
[[Category: Yao H]]
[[Category: Biofilm]]
[[Category: Electron transport]]
[[Category: Iron binding]]
[[Category: Iron mobilization]]
[[Category: Iron storage]]
[[Category: Oxidoreductase]]
[[Category: Protein-protein interaction inhibitor]]

Latest revision as of 18:17, 18 October 2023

1.75 A resolution structure of WT BfrB from Pseudomonas aeruginosa in complex with a protein-protein interaction inhibitor JAG-5-71.75 A resolution structure of WT BfrB from Pseudomonas aeruginosa in complex with a protein-protein interaction inhibitor JAG-5-7

Structural highlights

7k5e is a 12 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 1.75Å
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

Bacteria depend on a well-regulated iron homeostasis to survive adverse environments. A key component of the iron homeostasis machinery is the compartmentalization of Fe(3+) in bacterioferritin and its subsequent mobilization as Fe(2+) to satisfy metabolic requirements. In Pseudomonas aeruginosa Fe(3+) is compartmentalized in bacterioferritin (BfrB), and its mobilization to the cytosol requires binding of a ferredoxin (Bfd) to reduce the stored Fe(3+) and release the soluble Fe(2+). Blocking the BfrB-Bfd complex in P. aeruginosa by deletion of the bfd gene triggers an irreversible accumulation of Fe(3+) in BfrB, concomitant cytosolic iron deficiency and significant impairment of biofilm development. Herein we report that small molecules developed to bind BfrB at the Bfd binding site block the BfrB-Bfd complex, inhibit the mobilization of iron from BfrB in P. aeruginosa cells, elicit a bacteriostatic effect on planktonic cells, and are bactericidal to cells embedded in mature biofilms.

Small Molecule Inhibitors of the Bacterioferritin (BfrB)-Ferredoxin (Bfd) Complex Kill Biofilm-Embedded Pseudomonas aeruginosa Cells.,Soldano A, Yao H, Punchi Hewage AND, Meraz K, Annor-Gyamfi JK, Bunce RA, Battaile KP, Lovell S, Rivera M ACS Infect Dis. 2020 Dec 3. doi: 10.1021/acsinfecdis.0c00669. PMID:33269912[1]

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

See Also

References

  1. Soldano A, Yao H, Punchi Hewage AND, Meraz K, Annor-Gyamfi JK, Bunce RA, Battaile KP, Lovell S, Rivera M. Small Molecule Inhibitors of the Bacterioferritin (BfrB)-Ferredoxin (Bfd) Complex Kill Biofilm-Embedded Pseudomonas aeruginosa Cells. ACS Infect Dis. 2020 Dec 3. doi: 10.1021/acsinfecdis.0c00669. PMID:33269912 doi:http://dx.doi.org/10.1021/acsinfecdis.0c00669

7k5e, resolution 1.75Å

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