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1o7t
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Transferrins transport Fe3+ and other metal ions in mononuclear-binding | + | 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.]] | ||
| - | [[Category: Campopiano, D | + | [[Category: Campopiano, D J.]] |
[[Category: Guo, M.]] | [[Category: Guo, M.]] | ||
| - | [[Category: Hunter, D | + | [[Category: Hunter, D J.B.]] |
| - | [[Category: Sadler, P | + | [[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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
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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
Page seeded by OCA on Thu Feb 21 14:14:27 2008
