9iig
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | '''Unreleased structure''' | ||
- | + | ==Cryo-EM structure of hetero-bacterioferritin SoBfr12 from Shewanella oneidensis== | |
+ | <StructureSection load='9iig' size='340' side='right'caption='[[9iig]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[9iig]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_oneidensis_MR-1 Shewanella oneidensis MR-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9IIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9IIG FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6Å</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=NA:SODIUM+ION'>NA</scene></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=9iig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9iig OCA], [https://pdbe.org/9iig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9iig RCSB], [https://www.ebi.ac.uk/pdbsum/9iig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9iig ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q8EHV0_SHEON Q8EHV0_SHEON] Iron-storage protein, whose ferroxidase center binds Fe(2+), oxidizes it using dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the BFR protein shell.[PIRNR:PIRNR002560] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Iron-storage bacterioferritins (Bfrs), existing in either homo- or hetero-multimeric form, play a crucial role in iron homeostasis. While the structure and function of homo-multimeric bacterioferritins (homo-Bfrs) have been extensively studied, little is known about the assembly, distinctive characteristics, or evolutionary adaptations of hetero-multimeric bacterioferritins (hetero-Bfrs). Here, the cryo-EM structure and functional characterization of a bacterial hetero-Bfr (SoBfr12) are reported. Compared to homo-Bfrs, although SoBfr12 exhibits a conserved spherical cage-like dodecahedron, its pores through which ions traverse exhibit substantially increased diversity. Importantly, the heterogeneity has significant impacts on sites for ion entry, iron oxidation, and reduction. Moreover, evolutionary analyses reveal that hetero-Bfrs may represent a new class within the Bfr subfamily, consisting of two different types that may have evolved from homo-Bfr through tandem duplication and directly from ferritin (Ftn) via dispersed duplication, respectively. These results reveal remarkable structural and functional features of a hetero-Bfr, enabling the rational design of nanocages for enhanced iron-storing efficiency and for other specific purposes, such as drug delivery vehicles and nanozymes. | ||
- | + | Unveiling Structural Heterogeneity and Evolutionary Adaptations of Heteromultimeric Bacterioferritin Nanocages.,Li Y, Wang W, Wang W, Zhang X, Chen J, Gao H Adv Sci (Weinh). 2025 Apr 1:e2409957. doi: 10.1002/advs.202409957. PMID:40167232<ref>PMID:40167232</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 9iig" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | == References == |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Shewanella oneidensis MR-1]] | ||
+ | [[Category: Chen JH]] | ||
+ | [[Category: Gao HC]] | ||
+ | [[Category: Li YX]] |
Current revision
Cryo-EM structure of hetero-bacterioferritin SoBfr12 from Shewanella oneidensis
|