5ZUR

Achromobacter Dh1f Bacterioferritin

Summary for 5ZUR

• Entry DOI: 10.2210/pdb5zur/pdb
• Descriptor: Bacterioferritin, PROTOPORPHYRIN IX CONTAINING FE, FE (II) ION, ... (7 entities in total)
• Functional Keywords: bacteriferritin, heme, iron, metal binding protein
• Biological source: Achromobacter sp. DH1f
• Total number of polymer chains: 3
• Total formula weight: 57901.17

Authors

Dwivedy, A.,Jha, B.,Singh, K.H.,Ahmed, M.,Ashraf, A.,Kumar, D.,Biswal, B.K. (deposition date: 2018-05-08, release date: 2018-09-05, Last modification date: 2023-11-22)

Primary citation

Dwivedy, A.,Jha, B.,Singh, K.H.,Ahmad, M.,Ashraf, A.,Kumar, D.,Biswal, B.K.
Serendipitous crystallization and structure determination of bacterioferritin from Achromobacter.
Acta Crystallogr F Struct Biol Commun, 74:558-566, 2018

PubMed Abstract: Bacterioferritins (Bfrs) are ferritin-like molecules with a hollow spherical 24-mer complex design that are unique to bacterial and archaeal species. They play a critical role in storing iron(III) within the complex at concentrations much higher than the feasible solubility limits of iron(III), thus maintaining iron homeostasis within cells. Here, the crystal structure of bacterioferritin from Achromobacter (Ach Bfr) that crystallized serendipitously during a crystallization attempt of an unrelated mycobacterial protein is reported at 1.95 Å resolution. Notably, Fe atoms were bound to the structure along with a porphyrin ring sandwiched between the subunits of a dimer. Furthermore, the dinuclear ferroxidase center of Ach Bfr has only a single iron bound, in contrast to the two Fe atoms in other Bfrs. The structure of Ach Bfr clearly demonstrates the substitution of a glutamate residue, which is involved in the interaction with the second Fe atom, by a threonine and the consequent absence of another Fe atom there. The iron at the dinuclear center has a tetravalent coordination, while a second iron with a hexavalent coordination was found within the porphyrin ring, generating a heme moiety. Achromobacter spp. are known opportunistic pathogens; this structure enhances the current understanding of their iron metabolism and regulation, and importantly will be useful in the design of small-molecule inhibitors against this protein through a structure-guided approach.

PubMed: 30198888
DOI: 10.1107/S2053230X18009809

Experimental method

X-RAY DIFFRACTION (1.95 Å)