1o7t
METAL NANOCLUSTERS BOUND TO THE FERRIC BINDING PROTEIN FROM NEISSERIA GONORRHOEAE.
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| 1o7t, resolution 1.65Å | |||||||||||||
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| Sites: | HF1 | ||||||||||||
| Ligands: | HF5, HF3 and PHF | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
Transferrins transport Fe3+ and other metal ions in mononuclear-binding sites. We present the first evidence that a member of the transferrin superfamily is able to recognize multi-nuclear oxo-metal clusters, small mineral fragments that are the most abundant forms of many metals in the environment. We show that the ferric ion-binding protein from Neisseria gonorrhoeae (nFbp) readily binds clusters of Fe3+, Ti4+, Zr4+ or Hf4+ in solution. The 1.7 A resolution crystal structure of Hf-nFbp reveals three distinct types of clusters in an open, positively charged cleft between two hinged protein domains. A di-tyrosyl cluster nucleation motif (Tyr195-Tyr196) is situated at the bottom of this cleft and binds either a trinuclear oxo-Hf cluster, which is capped by phosphate, or a pentanuclear cluster, which in turn can be capped with phosphate. This first high-resolution structure of a protein-mineral interface suggests a novel metal-uptake mechanism and provides a model for protein-mediated mineralization/dissimilation, which plays a critical role in geochemical processes.
About this Structure
1O7T is a Single protein structure of sequence from Neisseria gonorrhoeae. Full crystallographic information is available from OCA.
Reference
A novel protein-mineral interface., Alexeev D, Zhu H, Guo M, Zhong W, Hunter DJ, Yang W, Campopiano DJ, Sadler PJ, Nat Struct Biol. 2003 Apr;10(4):297-302. PMID:12598891
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