Source:
Generated By: https://synbiohub.org/public/igem/igem2sbol/1
Created by: Johann Bauerfeind
Date created: 2014-09-12 11:00:00
Date modified: 2015-07-22 02:12:09
Bacterioferritin (BFR)
| Types | DnaRegion |
| Roles | Coding CDS |
| Sequences | BBa_K1438000_sequence (Version 1) |
Description
Bacterioferritins are the E. coli cells natural iron storage proteins. These hollow nearly spherical protein shells detoxify the cell by sequestering excessive iron and forming Iron(III)hydroxid-oxide particels.Bacterioferritin is an heam containing bacterial ferritin. Each heme is bound in a pocked formed by the interface between a pair of symmetry-related subunits [1]. However, it was investigated that these heme groups may be involved in the release of iron out of the ferritin iron core by forming an heme-mediated electron transfer to reduce immobilized Fe3+ to more soluble Fe2+.
[1] Frolow F, Kalb AJ, Yariv J. Structure of a unique twofold symmetric
haem-binding site. Nat Struct Biol. 1994 Jul;1(7):453-60. PubMed PMID: 7664064.
[2] Yao H, Wang Y, Lovell S, Kumar R, Ruvinsky AM, Battaile KP, Vakser IA, Rivera
M. The structure of the BfrB-Bfd complex reveals protein-protein interactions
enabling iron release from bacterioferritin. J Am Chem Soc. 2012 Aug
15;134(32):13470-81. doi: 10.1021/ja305180n. Epub 2012 Aug 1. PubMed PMID:
22812654; PubMed Central PMCID: PMC3428730.
Notes
For any metal nanoparticles built inside of BFR it would be beneficary to remove any heme groups in order to prevent unloading of BFR by heme-mediated electron transfer.Source
Bacterioferritin from E. coli Nissle 1917 genomic DNA. Amplified by using PCR and cloned into pQE80L| Sequence Annotation | Location | Component / Role(s) |
| start codon His Tag stop codon BioBrick | 1,3 13,30 511,513 1,513 | feature/start start_codon tag feature/tag feature/stop stop_codon engineered_region feature/BioBrick |