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6e6q

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1.20 A resolution structure of the C-terminally truncated [2Fe-2S] ferredoxin (Bfd) from Pseudomonas aeruginosa

Structural highlights

6e6q is a 2 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9HY80_PSEAE

Publication Abstract from PubMed

Mobilization of iron from bacterioferritin (BfrB) requires specific interactions with a [2Fe-2S] ferredoxin (Bfd). Blocking the BfrB:Bfd interaction results in irreversible iron accumulation in BfrB and iron deficiency in the cytosol [Eshelman, K., et al. (2017) Metallomics 9, 646-659]. The only known Bfd structure, which was obtained in complex with BfrB (Protein Data Bank entry 4E6K ), indicated a new fold and suggested that the stability of Bfd is aided by an anion binding site consisting of R26, R29, and K46. We investigated the Bfd fold using site-directed mutagenesis, X-ray crystallography, and biochemistry in solution. The X-ray structure, which is nearly identical to that of Bfd in the BfrB:Bfd complex, shows that the [2Fe-2S] cluster preorganizes residues at the BfrB:Bfd interface into a structure complementary to the Bfd binding site on BfrB. Studies in solution showed rapid loss of the [2Fe-2S] cluster at a low ionic strength but higher stability with an increasing ionic strength, thus supporting a structural anion binding site. Structures of the R26E and R26E/K46Y mutants are nearly identical to that of Bfd, except for a new network of hydrogen bonds stabilizing the region encompassing the former anion binding site. The stability of the R26E and R26E/K46Y mutants, which is weakly and completely independent of solution ionic strength, respectively, corroborates that Bfd requires an anion binding site. The mutations, which caused only small changes to the strength of the BfrB:Bfd interaction and mobilization of iron from BfrB, indicate that the anion binding site in Bfd serves primarily a structural role.

Bfd, a New Class of [2Fe-2S] Protein That Functions in Bacterial Iron Homeostasis, Requires a Structural Anion Binding Site.,Wijerathne H, Yao H, Wang Y, Lovell S, Battaile KP, Rivera M Biochemistry. 2018 Sep 13. doi: 10.1021/acs.biochem.8b00823. PMID:30183257^[1]

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

References

↑ Wijerathne H, Yao H, Wang Y, Lovell S, Battaile KP, Rivera M. Bfd, a New Class of [2Fe-2S] Protein That Functions in Bacterial Iron Homeostasis, Requires a Structural Anion Binding Site. Biochemistry. 2018 Sep 13. doi: 10.1021/acs.biochem.8b00823. PMID:30183257 doi:http://dx.doi.org/10.1021/acs.biochem.8b00823

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/6e6q"

@@ Line 1: / Line 1: @@
 ==1.20 A resolution structure of the C-terminally truncated [2Fe-2S] ferredoxin (Bfd) from Pseudomonas aeruginosa==
-<StructureSection load='6e6q' size='340' side='right' caption='[[6e6q]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
+<StructureSection load='6e6q' size='340' side='right'caption='[[6e6q]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6e6q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E6Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E6Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6e6q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E6Q FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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]] 1.2&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bfd, AO896_12000, AO964_01120, AOY09_04877, C8257_08100, CAZ03_03910, CAZ10_19915, CGU42_05470, CSB93_2785, PAERUG_E15_London_28_01_14_09195, PAMH19_1562, RW109_RW109_02290 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></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=6e6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e6q OCA], [http://pdbe.org/6e6q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e6q RCSB], [http://www.ebi.ac.uk/pdbsum/6e6q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e6q ProSAT]</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=6e6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e6q OCA], [https://pdbe.org/6e6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e6q RCSB], [https://www.ebi.ac.uk/pdbsum/6e6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e6q ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9HY80_PSEAE Q9HY80_PSEAE]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 19: @@
 </div>
 <div class="pdbe-citations 6e6q" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Battaile, K P]]
+[[Category: Large Structures]]
-[[Category: Lovell, S]]
+[[Category: Pseudomonas aeruginosa]]
-[[Category: Rivera, M]]
+[[Category: Battaile KP]]
-[[Category: Wang, Y]]
+[[Category: Lovell S]]
-[[Category: Wijerathne, H]]
+[[Category: Rivera M]]
-[[Category: Yao, H]]
+[[Category: Wang Y]]
-[[Category: Anion binding site]]
+[[Category: Wijerathne H]]
-[[Category: Bfd]]
+[[Category: Yao H]]
-[[Category: Electron transport]]
-[[Category: Iron mobilization]]

6e6q

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Current revision

1.20 A resolution structure of the C-terminally truncated [2Fe-2S] ferredoxin (Bfd) from Pseudomonas aeruginosa

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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