X-ray structure of recombinant horse L-chain apoferritin at 2.0 Å resolution: implications for stability and function

Gallois, B.; d’Estaintot, Béatrice Langlois; Michaux, Marie-Anges; Dautant, Alain; Granier, T.; Précigoux, G.; Soruco, José-Antonio; Roland, Francine; Chavas-Alba, Octavío; Herbas, Adelina; Crichton, Robert R.

doi:10.1007/s007750050143

Cited by 64 publications

(57 citation statements)

References 1 publication

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Their molecules are assemblies of 24 structurally equivalent protein chains or subunits related in 432 symmetry and forming a nearly spherical shell ( Fig. 1A) with an 80-Å diameter iron storage cavity (7,(12)(13)(14)(15)(16)(17). The protein subunits are folded as four helix bundles about 27 Å long with a fifth shorter helix lying at about 60°to the bundle (Fig.…”

mentioning

confidence: 99%

“…The three-dimensional structures of native or recombinant ferritins from human (12,17), horse (12,16), rat (17), mouse (20), frog (14,15), and E. coli (13) have been determined, but most of these are L ferritins, and relatively little high resolution information has been obtained on the structures of the di-iron centers of H-type ferritins. Moreover, the iron centers in the animal H ferritins (e.g.…”

mentioning

confidence: 99%

“…The function of the L subunit seems to be to provide a site that favors the fourelectron reduction of dioxygen. This site consists of clusters of Glu residues located on the L-subunit inner surface and acts as a nucleation center for the formation of mineral, thus stimulating its deposition within the inner cavity (7,16). EcBfr and EcFtnA each consist of just one type of subunit with features more reminiscent of H subunits than L subunits (1,13,17,18 …”

mentioning

confidence: 99%

See 2 more Smart Citations

Insights into the Effects on Metal Binding of the Systematic Substitution of Five Key Glutamate Ligands in the Ferritin of Escherichia coli

Stillman

Connolly

Latimer

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

Living organisms take advantage of the catalytic and redox properties of metals to drive a wide range of vital biological processes. This exploitation of metals is mainly enabled by incorporating them into proteins in various forms. An important class of metal proteins are those that contain dinuclear metal (or dimetal) centers at their active sites (1-4). A common feature of this functionally diverse family is that each dimetal center is embedded in a bundle of four or more helices in a way that enables the binding of dioxygen and/or hydrogen peroxide. With the exception of the dioxygen carrier hemerythrin, in which the metal ligands are found in the motifs HXXXE and HXXXXD, known dimetal centers have either one or two ligand sets within the motif EXXH. Each EXXH motif is located in a separate helix with the Glu residue acting as a bridging ligand between iron atoms, often together with either a second Glu (within a second EXXH motif) or one or more H 2 O, OH Ϫ , or O 2Ϫ

show abstract

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Insights into the Effects on Metal Binding of the Systematic Substitution of Five Key Glutamate Ligands in the Ferritin of Escherichia coli

Stillman

Connolly

Latimer

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Ferritin is responsible for the storage and transfer of ferric ions, that can be toxic to the organism in higher doses [19]. The apoferritin protein shell is in the form of a hollow rhombic dodecahedron, created by 24 roughly cylindrical subunits of two types [20]. Its most important property is its responsiveness to the surrounding proton concentration, which allows for a very simple encapsulation protocol [21].…”

Section: Apoferritin -Basic Informationmentioning

confidence: 99%

“…The structure of animal apoferritin protein shell is composed of two types of 24 subunits -heavy (H) and light (L) -differing by the molecular weight -21 and 19 kDa, respectively [20], with 53% sequence identity [45]. The H and L sequences are very heterogeneous between (apo)ferritins from different tissues within the same animal species with only 40-50% homology.…”

Section: Apoferritin Structurementioning

confidence: 99%

Apoferritin: protein nanocarrier for targeted delivery

Dostálová¹,

Heger²,

Kudr³

et al. 2015

Nano Based Drug Delivery

View full text Add to dashboard Cite

Evidence of new cadmium binding sites in recombinant horse L-chain ferritin by anomalous Fourier difference map calculation

et al. 1998

Self Cite

View full text Add to dashboard Cite

We refined the structure of the tetragonal form of recombinant horse L-chain apoferritin to 2.0 A and we compared it with that of the cubic form previously refined to the same resolution. The major differences between the two structures concern the cadmium ions bound to the residues E130 at the threefold axes of the molecule. Taking advantage of the significant anomalous signal (f" = 3.6 e-) of cadmium at 1.375 A, the wavelength used here, we performed anomalous Fourier difference maps with the refined model phases. These maps reveal the positions of anomalous scatterers at different locations in the structure. Among these, some are found near residues that were known previously to bind metal ions, C48, E57, C126, D127, E130, and H132. But new cadmium binding sites are evidenced near residues E53, E56, E57, E60, and H114, which were suggested to be involved in the iron loading process. The quality of the anomalous Fourier difference map increases significantly with noncrystallographic symmetry map averaging. Such maps reveal density peaks that fit the positions of Met and Cys sulfur atoms, which are weak anomalous scatterers (f" = 0.44 e-).

show abstract

X-ray structure of recombinant horse L-chain apoferritin at 2.0 Å resolution: implications for stability and function

Cited by 64 publications

References 1 publication

Insights into the Effects on Metal Binding of the Systematic Substitution of Five Key Glutamate Ligands in the Ferritin of Escherichia coli

Insights into the Effects on Metal Binding of the Systematic Substitution of Five Key Glutamate Ligands in the Ferritin of Escherichia coli

Apoferritin: protein nanocarrier for targeted delivery

Evidence of new cadmium binding sites in recombinant horse L-chain ferritin by anomalous Fourier difference map calculation

Contact Info

Product

Resources

About