1O7T
Metal nanoclusters bound to the Ferric Binding Protein from Neisseria gonorrhoeae.
Summary for 1O7T
Entry DOI | 10.2210/pdb1o7t/pdb |
Related | 1D9Y |
Descriptor | IRON BINDING PROTEIN, HF OXO CLUSTER HF5, SMALLEST HF-OXO-PHOSPHATE CLUSTER HF3, ... (5 entities in total) |
Functional Keywords | metal-binding protein, periplasmic ferric binding protein, hafnium, metal-oxo cluster, metal binding protein |
Biological source | NEISSERIA GONORRHOEAE |
Total number of polymer chains | 9 |
Total formula weight | 313992.53 |
Authors | Alexeev, D.,Zu, H.,Guo, M.,Zhong, W.,Hunter, D.J.B.,Yang, W.,Campopiano, D.J.,Sadler, P.J. (deposition date: 2002-11-12, release date: 2003-02-27, Last modification date: 2023-12-13) |
Primary citation | Alexeev, D.,Zhu, H.,Guo, M.,Zhong, W.,Hunter, D.J.,Yang, W.,Campopiano, D.J.,Sadler, P.J. A novel protein-mineral interface. Nat. Struct. Biol., 10:297-302, 2003 Cited by PubMed Abstract: 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. PubMed: 12598891DOI: 10.1038/nsb903 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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