1r1n
From Proteopedia
(New page: 200px<br /><applet load="1r1n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r1n, resolution 1.74Å" /> '''Tri-nuclear oxo-iron...) |
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| - | [[Image:1r1n.gif|left|200px]]<br /><applet load="1r1n" size=" | + | [[Image:1r1n.gif|left|200px]]<br /><applet load="1r1n" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r1n, resolution 1.74Å" /> | caption="1r1n, resolution 1.74Å" /> | ||
'''Tri-nuclear oxo-iron clusters in the ferric binding protein from N. gonorrhoeae'''<br /> | '''Tri-nuclear oxo-iron clusters in the ferric binding protein from N. gonorrhoeae'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report a set of three 1.8-1.9 A resolution X-ray crystal structures of | + | We report a set of three 1.8-1.9 A resolution X-ray crystal structures of Neisseria gonorrhoeae Fbp (ferric-ion binding protein): (i) open-cleft apo-Fbp containing bound phosphate, (ii) open-cleft mono-Fe Fbp capped by nitrilotriacetate, and (iii) open-cleft trinuclear oxo-iron Fbp, the first structure of an iron-cluster adduct of a transferrin. The nine independent molecules in the unit cells provide 'snapshots' of the versatile dynamic structural roles of the conserved dityrosyl iron-binding motif (Tyr195-Tyr196) which control the capture and, possibly, processing of iron. These findings have implications for understanding bacterial iron acquisition and dissimilation, and organic/mineral interfaces. |
==About this Structure== | ==About this Structure== | ||
| - | 1R1N 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 CNB, CN1 and CNF as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1R1N 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 <scene name='pdbligand=CNB:'>CNB</scene>, <scene name='pdbligand=CN1:'>CN1</scene> and <scene name='pdbligand=CNF:'>CNF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1N OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Alexeev, D.]] | [[Category: Alexeev, D.]] | ||
| - | [[Category: Campopiano, D | + | [[Category: Campopiano, D J.]] |
| - | [[Category: Hunter, D | + | [[Category: Hunter, D J.]] |
| - | [[Category: Sadler, P | + | [[Category: Sadler, P J.]] |
[[Category: Zhu, H.]] | [[Category: Zhu, H.]] | ||
[[Category: CN1]] | [[Category: CN1]] | ||
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[[Category: iron binding protein]] | [[Category: iron binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:02 2008'' |
Revision as of 12:46, 21 February 2008
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Tri-nuclear oxo-iron clusters in the ferric binding protein from N. gonorrhoeae
Overview
We report a set of three 1.8-1.9 A resolution X-ray crystal structures of Neisseria gonorrhoeae Fbp (ferric-ion binding protein): (i) open-cleft apo-Fbp containing bound phosphate, (ii) open-cleft mono-Fe Fbp capped by nitrilotriacetate, and (iii) open-cleft trinuclear oxo-iron Fbp, the first structure of an iron-cluster adduct of a transferrin. The nine independent molecules in the unit cells provide 'snapshots' of the versatile dynamic structural roles of the conserved dityrosyl iron-binding motif (Tyr195-Tyr196) which control the capture and, possibly, processing of iron. These findings have implications for understanding bacterial iron acquisition and dissimilation, and organic/mineral interfaces.
About this Structure
1R1N is a Single protein structure of sequence from Neisseria gonorrhoeae with , and as ligands. Full crystallographic information is available from OCA.
Reference
Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif., Zhu H, Alexeev D, Hunter DJ, Campopiano DJ, Sadler PJ, Biochem J. 2003 Nov 15;376(Pt 1):35-41. PMID:13129433
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