3ERZ

Directing Noble Metal Ion Chemistry within a Designed Ferritin Protein. Mercury Ions on the Three-Fold Channel

Summary for 3ERZ

• Entry DOI: 10.2210/pdb3erz/pdb
• Related: 2Z6M 3ES3
• Descriptor: Ferritin heavy chain, (4S)-2-METHYL-2,4-PENTANEDIOL, MERCURY (II) ION, ... (6 entities in total)
• Functional Keywords: ferritin mutant, nanoparticle, 3-fold channel, mercury ions, iron, iron storage, metal-binding, oxidoreductase, phosphoprotein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 12
• Total formula weight: 257841.65

Authors

Di Costanzo, L.,Christianson, D.W. (deposition date: 2008-10-03, release date: 2008-10-21, Last modification date: 2023-12-27)

Primary citation

Butts, C.A.,Swift, J.,Kang, S.G.,Di Costanzo, L.,Christianson, D.W.,Saven, J.G.,Dmochowski, I.J.
Directing noble metal ion chemistry within a designed ferritin protein.
Biochemistry, 47:12729-12739, 2008

PubMed Abstract: Human H ferritin (HuHF) assembles from 24 four-helix bundles to form an approximately 500 kDa protein with an 8 nm internal cavity. HuHF provides a useful model for studying the transport of metal ions in solution to buried reaction sites in proteins. In this study, HuHF was redesigned to facilitate noble metal ion (Au(3+), Ag(+)) binding, reduction, and nanoparticle formation within the cavity. Computationally determined amino acid substitutions were targeted at four external and four internal surface sites. A variant with a total of 96 cysteines and histidines removed from the exterior surface and 96 non-native cysteines added to the interior surface retained wild-type stability and structure, as confirmed by X-ray crystallography, and promoted the formation of silver or gold nanoparticles within the protein cavity. Crystallographic studies with HuHF variants provide insight into how ferritins control access of metal ions to interior residues that perform chemistry.

PubMed: 18991401
DOI: 10.1021/bi8016735

Experimental method

X-RAY DIFFRACTION (3.056 Å)