1jax

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(New page: 200px<br /><applet load="1jax" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jax, resolution 1.80&Aring;" /> '''Structure of Coenzym...)
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'''Structure of Coenzyme F420H2:NADP+ Oxidoreductase (FNO)'''<br />
'''Structure of Coenzyme F420H2:NADP+ Oxidoreductase (FNO)'''<br />
==Overview==
==Overview==
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Cofactor F420 is a 5'-deazaflavin derivative first discovered in, methanogenic archaea but later found also to be present in some bacteria., As a coenzyme, it is involved in hydride transfer reactions and as a, prosthetic group in the DNA photolyase reaction. We report here for the, first time on the crystal structure of an F420-dependent oxidoreductase, bound with F420. The structure of F420H2:NADP+ oxidoreductase resolved to, 1.65 A contains two domains: an N-terminal domain characteristic of a, dinucleotide-binding Rossmann fold and a smaller C-terminal domain. The, nicotinamide and the deazaflavin part of the two coenzymes are bound in, the cleft between the domains such that the Si-faces of both face each, other at a distance of 3.1 A, which is optimal for hydride transfer., Comparison of the structures bound with and without substrates reveals, that of the two substrates NADP has to bind first, the binding being, associated with an induced fit.
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Cofactor F420 is a 5'-deazaflavin derivative first discovered in methanogenic archaea but later found also to be present in some bacteria. As a coenzyme, it is involved in hydride transfer reactions and as a prosthetic group in the DNA photolyase reaction. We report here for the first time on the crystal structure of an F420-dependent oxidoreductase bound with F420. The structure of F420H2:NADP+ oxidoreductase resolved to 1.65 A contains two domains: an N-terminal domain characteristic of a dinucleotide-binding Rossmann fold and a smaller C-terminal domain. The nicotinamide and the deazaflavin part of the two coenzymes are bound in the cleft between the domains such that the Si-faces of both face each other at a distance of 3.1 A, which is optimal for hydride transfer. Comparison of the structures bound with and without substrates reveals that of the two substrates NADP has to bind first, the binding being associated with an induced fit.
==About this Structure==
==About this Structure==
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1JAX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with NA and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JAX OCA].
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1JAX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JAX OCA].
==Reference==
==Reference==
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[[Category: rossman fold]]
[[Category: rossman fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:22:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:20:37 2008''

Revision as of 11:20, 21 February 2008

Image:1jax.gif

1jax, resolution 1.80Å

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Structure of Coenzyme F420H2:NADP+ Oxidoreductase (FNO)

Overview

Cofactor F420 is a 5'-deazaflavin derivative first discovered in methanogenic archaea but later found also to be present in some bacteria. As a coenzyme, it is involved in hydride transfer reactions and as a prosthetic group in the DNA photolyase reaction. We report here for the first time on the crystal structure of an F420-dependent oxidoreductase bound with F420. The structure of F420H2:NADP+ oxidoreductase resolved to 1.65 A contains two domains: an N-terminal domain characteristic of a dinucleotide-binding Rossmann fold and a smaller C-terminal domain. The nicotinamide and the deazaflavin part of the two coenzymes are bound in the cleft between the domains such that the Si-faces of both face each other at a distance of 3.1 A, which is optimal for hydride transfer. Comparison of the structures bound with and without substrates reveals that of the two substrates NADP has to bind first, the binding being associated with an induced fit.

About this Structure

1JAX is a Single protein structure of sequence from Archaeoglobus fulgidus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structures of F420H2:NADP+ oxidoreductase with and without its substrates bound., Warkentin E, Mamat B, Sordel-Klippert M, Wicke M, Thauer RK, Iwata M, Iwata S, Ermler U, Shima S, EMBO J. 2001 Dec 3;20(23):6561-9. PMID:11726492

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