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4tod

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Revision as of 01:20, 19 January 2017

2.05A resolution structure of BfrB (D34F) from Pseudomonas aeruginosa

Structural highlights

4tod is a 24 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4to9, 4toa, 4tob, 4toc, 4toe, 4tof, 4tog, 4toh
Activity:	Ferroxidase, with EC number 1.16.3.1
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

X-ray crystallography, molecular dynamics (MD) simulations and biochemistry were utilized to investigate the effect of introducing hydrophobic interactions in the 4-fold (N148L and Q151L) and B-pores (D34F) of Pseudomonas aeruginosa bacterioferritin B (BfrB) on BfrB function. The structures show only local structural perturbations and confirm the anticipated hydrophobic interactions. Surprisingly, structures obtained after soaking crystals in Fe2+-containing crystallization solution revealed that although iron loads into the ferroxidase centers of the mutants, the side chains of ferroxidase ligands E51 and H130 do not reorganize to bind the iron ions, as is seen in the wt BfrB structures. Similar experiments with a double mutant (C89S/K96C) prepared to introduce changes outside the pores show competent ferroxidase centers that function akin to those in wt BfrB. MD simulations comparing wt BfrB with the D34F and N148L mutants show that the mutants exhibit significantly reduced flexibility, and reveal a network of concerted motions linking ferroxidase centers and 4-fold and B-pores, which are important for imparting ferroxidase centers in BfrB with the required flexibility to function efficiently. In agreement, the efficiency of Fe2+ oxidation and uptake of the 4-fold and B-pore mutants in solution is significantly compromised relative to wt or C89S/K96C BfrB. Finally, our structures show a large number of previously unknown iron binding sites in the interior cavity and B-pores of BfrB, which reveal in unprecedented detail conduits followed by iron and phosphate ions across the BfrB shell, as well as paths in the interior cavity that may facilitate nucleation of the iron phosphate mineral.

Concerted Motions Networking Pores and Distant Ferroxidase Centers Enable Bacterioferritin Function and Iron Traffic.,Yao H, Rui H, Kumar R, Eshelman K, Lovell S, Battaile KP, Im W, Rivera M Biochemistry. 2015 Jan 31. PMID:25640193^[1]

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

References

↑ Yao H, Rui H, Kumar R, Eshelman K, Lovell S, Battaile KP, Im W, Rivera M. Concerted Motions Networking Pores and Distant Ferroxidase Centers Enable Bacterioferritin Function and Iron Traffic. Biochemistry. 2015 Jan 31. PMID:25640193 doi:http://dx.doi.org/10.1021/bi501255r

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4tod"

@@ Line 1: / Line 1: @@
 ==2.05A resolution structure of BfrB (D34F) from Pseudomonas aeruginosa==
 <StructureSection load='4tod' size='340' side='right' caption='[[4tod]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4to9|4to9]], [[4toa|4toa]], [[4tob|4tob]], [[4toc|4toc]], [[4toe|4toe]], [[4tof|4tof]], [[4tog|4tog]], [[4toh|4toh]]</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tod RCSB], [http://www.ebi.ac.uk/pdbsum/4tod PDBsum]</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=4tod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tod OCA], [http://pdbe.org/4tod PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tod RCSB], [http://www.ebi.ac.uk/pdbsum/4tod PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tod ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4tod" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4tod

From Proteopedia

Revision as of 01:20, 19 January 2017

2.05A resolution structure of BfrB (D34F) from Pseudomonas aeruginosa

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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