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| | <StructureSection load='6e6r' size='340' side='right'caption='[[6e6r]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='6e6r' size='340' side='right'caption='[[6e6r]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6e6r]] is a 1 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=6E6R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E6R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6e6r]] is a 1 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=6E6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E6R 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]] 1.5Å</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 ([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=6e6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e6r OCA], [http://pdbe.org/6e6r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e6r RCSB], [http://www.ebi.ac.uk/pdbsum/6e6r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e6r 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=6e6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e6r OCA], [https://pdbe.org/6e6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e6r RCSB], [https://www.ebi.ac.uk/pdbsum/6e6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e6r ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9HY80_PSEAE Q9HY80_PSEAE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Battaile, K P]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Lovell, S]] | + | [[Category: Battaile KP]] |
| - | [[Category: Rivera, M]] | + | [[Category: Lovell S]] |
| - | [[Category: Wang, Y]] | + | [[Category: Rivera M]] |
| - | [[Category: Wijerathne, H]] | + | [[Category: Wang Y]] |
| - | [[Category: Yao, H]] | + | [[Category: Wijerathne H]] |
| - | [[Category: Anion binding site]]
| + | [[Category: Yao H]] |
| - | [[Category: Bfd]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Iron mobilization]]
| + | |
| Structural highlights
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.
See Also
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
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