1o7t
From Proteopedia
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==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 1O7T is a | + | 1O7T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae] with HF5, HF3 and PHF as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: HF1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O7T OCA]. |
==Reference== | ==Reference== | ||
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[[Category: periplasmic ferric binding protein]] | [[Category: periplasmic ferric binding protein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:11:45 2007'' |
Revision as of 13:06, 5 November 2007
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METAL NANOCLUSTERS BOUND TO THE FERRIC BINDING PROTEIN FROM NEISSERIA GONORRHOEAE.
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 with HF5, HF3 and PHF as ligands. Structure known Active Site: HF1. 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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