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1o7t

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==Overview==
==Overview==
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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.
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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==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Alexeev, D.]]
[[Category: Alexeev, D.]]
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[[Category: Campopiano, D.J.]]
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[[Category: Campopiano, D J.]]
[[Category: Guo, M.]]
[[Category: Guo, M.]]
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[[Category: Hunter, D.J.B.]]
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[[Category: Hunter, D J.B.]]
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[[Category: Sadler, P.J.]]
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[[Category: Sadler, P J.]]
[[Category: Yang, W.]]
[[Category: Yang, W.]]
[[Category: Zhong, W.]]
[[Category: Zhong, W.]]
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[[Category: periplasmic ferric binding protein]]
[[Category: periplasmic ferric binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:54:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:14:27 2008''

Revision as of 12:14, 21 February 2008


1o7t, resolution 1.65Å

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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 , and as ligands. Known structural/functional Site: . 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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