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==1.90 A resolution structure of WT BfrB from Pseudomonas aeruginosa in complex with a protein-protein interaction inhibitor KM-5-50== | ==1.90 A resolution structure of WT BfrB from Pseudomonas aeruginosa in complex with a protein-protein interaction inhibitor KM-5-50== | ||
<StructureSection load='7k5f' size='340' side='right'caption='[[7k5f]]' scene=''> | <StructureSection load='7k5f' size='340' side='right'caption='[[7k5f]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K5F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7K5F FirstGlance]. <br> | <table><tr><td colspan='2'>[[7k5f]] 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=7K5F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7K5F FirstGlance]. <br> | ||
</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=7k5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k5f OCA], [http://pdbe.org/7k5f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7k5f RCSB], [http://www.ebi.ac.uk/pdbsum/7k5f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7k5f ProSAT]</span></td></tr> | </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=VXP:4-{[(3-chloro-5-hydroxyphenyl)methyl]amino}-1H-isoindole-1,3(2H)-dione'>VXP</scene></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='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'>[http://proteopedia.org/fgij/fg.htm?mol=7k5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k5f OCA], [http://pdbe.org/7k5f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7k5f RCSB], [http://www.ebi.ac.uk/pdbsum/7k5f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7k5f ProSAT]</span></td></tr> | |||
</table> | </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] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:33269912</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7k5f" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ferroxidase]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Annor-Gyamfi | [[Category: Pseae]] | ||
[[Category: Battaile | [[Category: Annor-Gyamfi, J K]] | ||
[[Category: Bunce | [[Category: Battaile, K P]] | ||
[[Category: Lovell S]] | [[Category: Bunce, R A]] | ||
[[Category: Meraz K]] | [[Category: Lovell, S]] | ||
[[Category: Punchi-Hewage A]] | [[Category: Meraz, K]] | ||
[[Category: Rivera M]] | [[Category: Punchi-Hewage, A]] | ||
[[Category: Soldano A]] | [[Category: Rivera, M]] | ||
[[Category: Yao H]] | [[Category: Soldano, A]] | ||
[[Category: Yao, H]] | |||
[[Category: Biofilm]] | |||
[[Category: Electron transport]] | |||
[[Category: Iron binding]] | |||
[[Category: Iron mobilization]] | |||
[[Category: Iron storage]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Protein-protein interaction inhibitor]] | |||
Revision as of 11:30, 20 January 2021
1.90 A resolution structure of WT BfrB from Pseudomonas aeruginosa in complex with a protein-protein interaction inhibitor KM-5-501.90 A resolution structure of WT BfrB from Pseudomonas aeruginosa in complex with a protein-protein interaction inhibitor KM-5-50
Structural highlights
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 PubMedBacteria 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. References
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