Crystal structure of Cu2+ binding to Dendrorhynchus zhejiangensis ferritinCrystal structure of Cu2+ binding to Dendrorhynchus zhejiangensis ferritin

Structural highlights

8hct is a 1 chain structure with sequence from Dendrorhynchus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.26Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A8F4Y4C2_9BILA Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.[ARBA:ARBA00025111] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.[RuleBase:RU361145]

Publication Abstract from PubMed

Ferritin with a highly symmetrical cage-like structure is not only key in the reversible storage of iron in efficient ferroxidase activity; it also provides unique coordination environments for the conjugation of heavy metal ions other than those associated with iron. However, research regarding the effect of these bound heavy metal ions on ferritin is scarce. In the present study, we prepared a marine invertebrate ferritin from Dendrorhynchus zhejiangensis (DzFer) and found that it could withstand extreme pH fluctuation. We then demonstrated its capacity to interact with Ag(+) or Cu(2+) ions using various biochemical and spectroscopic methods and X-ray crystallography. Structural and biochemical analyses revealed that both Ag(+) and Cu(2+) were able to bind to the DzFer cage via metal-coordination bonds and that their binding sites were mainly located inside the three-fold channel of DzFer. Furthermore, Ag(+) was shown to have a higher selectivity for sulfur-containing amino acid residues and appeared to bind preferentially at the ferroxidase site of DzFer as compared with Cu(2+). Thus, it is far more likely to inhibit the ferroxidase activity of DzFer. The results provide new insights into the effect of heavy metal ions on the iron-binding capacity of a marine invertebrate ferritin.

Structural and Biochemical Characterization of Silver/Copper Binding by Dendrorhynchus zhejiangensis Ferritin.,Huo C, Ming T, Wu Y, Huan H, Qiu X, Lu C, Li Y, Zhang Z, Han J, Su X Polymers (Basel). 2023 Mar 3;15(5):1297. doi: 10.3390/polym15051297. PMID:36904538[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Huo C, Ming T, Wu Y, Huan H, Qiu X, Lu C, Li Y, Zhang Z, Han J, Su X. Structural and Biochemical Characterization of Silver/Copper Binding by Dendrorhynchus zhejiangensis Ferritin. Polymers (Basel). 2023 Mar 3;15(5):1297. PMID:36904538 doi:10.3390/polym15051297

8hct, resolution 2.26Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA