1jju

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(New page: 200px<br /><applet load="1jju" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jju, resolution 2.05&Aring;" /> '''Structure of a Quino...)
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[[Image:1jju.gif|left|200px]]<br /><applet load="1jju" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jju.gif|left|200px]]<br /><applet load="1jju" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jju, resolution 2.05&Aring;" />
caption="1jju, resolution 2.05&Aring;" />
'''Structure of a Quinohemoprotein Amine Dehydrogenase with a Unique Redox Cofactor and Highly Unusual Crosslinking'''<br />
'''Structure of a Quinohemoprotein Amine Dehydrogenase with a Unique Redox Cofactor and Highly Unusual Crosslinking'''<br />
==Overview==
==Overview==
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The crystal structure of the heterotrimeric quinohemoprotein amine, dehydrogenase from Paracoccus denitrificans has been determined at 2.05-A, resolution. Within an 82-residue subunit is contained an unusual redox, cofactor, cysteine tryptophylquinone (CTQ), consisting of an, orthoquinone-modified tryptophan side chain covalently linked to a nearby, cysteine side chain. The subunit is surrounded on three sides by a, 489-residue, four-domain subunit that includes a diheme cytochrome c. Both, subunits sit on the surface of a third subunit, a 337-residue seven-bladed, beta-propeller that forms part of the enzyme active site. The small, catalytic subunit is internally crosslinked by three highly unusual, covalent cysteine to aspartic or glutamic acid thioether linkages in, addition to the cofactor crossbridge. The catalytic function of the enzyme, as well as the biosynthesis of the unusual catalytic subunit is discussed.
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The crystal structure of the heterotrimeric quinohemoprotein amine dehydrogenase from Paracoccus denitrificans has been determined at 2.05-A resolution. Within an 82-residue subunit is contained an unusual redox cofactor, cysteine tryptophylquinone (CTQ), consisting of an orthoquinone-modified tryptophan side chain covalently linked to a nearby cysteine side chain. The subunit is surrounded on three sides by a 489-residue, four-domain subunit that includes a diheme cytochrome c. Both subunits sit on the surface of a third subunit, a 337-residue seven-bladed beta-propeller that forms part of the enzyme active site. The small catalytic subunit is internally crosslinked by three highly unusual covalent cysteine to aspartic or glutamic acid thioether linkages in addition to the cofactor crossbridge. The catalytic function of the enzyme as well as the biosynthesis of the unusual catalytic subunit is discussed.
==About this Structure==
==About this Structure==
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1JJU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with NA, HEM and TBU as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JJU OCA].
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1JJU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=TBU:'>TBU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJU OCA].
==Reference==
==Reference==
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[[Category: Paracoccus denitrificans]]
[[Category: Paracoccus denitrificans]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Chen, Z.W.]]
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[[Category: Chen, Z W.]]
[[Category: Datta, S.]]
[[Category: Datta, S.]]
[[Category: Ikeda, T.]]
[[Category: Ikeda, T.]]
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[[Category: Kawaguchi, K.]]
[[Category: Kawaguchi, K.]]
[[Category: Kuroda, S.]]
[[Category: Kuroda, S.]]
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[[Category: Mathews, F.S.]]
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[[Category: Mathews, F S.]]
[[Category: Mori, Y.]]
[[Category: Mori, Y.]]
[[Category: Okajima, T.]]
[[Category: Okajima, T.]]
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[[Category: quinohemoprotein]]
[[Category: quinohemoprotein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:19:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:28 2008''

Revision as of 11:23, 21 February 2008


1jju, resolution 2.05Å

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Structure of a Quinohemoprotein Amine Dehydrogenase with a Unique Redox Cofactor and Highly Unusual Crosslinking

Overview

The crystal structure of the heterotrimeric quinohemoprotein amine dehydrogenase from Paracoccus denitrificans has been determined at 2.05-A resolution. Within an 82-residue subunit is contained an unusual redox cofactor, cysteine tryptophylquinone (CTQ), consisting of an orthoquinone-modified tryptophan side chain covalently linked to a nearby cysteine side chain. The subunit is surrounded on three sides by a 489-residue, four-domain subunit that includes a diheme cytochrome c. Both subunits sit on the surface of a third subunit, a 337-residue seven-bladed beta-propeller that forms part of the enzyme active site. The small catalytic subunit is internally crosslinked by three highly unusual covalent cysteine to aspartic or glutamic acid thioether linkages in addition to the cofactor crossbridge. The catalytic function of the enzyme as well as the biosynthesis of the unusual catalytic subunit is discussed.

About this Structure

1JJU is a Protein complex structure of sequences from Paracoccus denitrificans with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking., Datta S, Mori Y, Takagi K, Kawaguchi K, Chen ZW, Okajima T, Kuroda S, Ikeda T, Kano K, Tanizawa K, Mathews FS, Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14268-73. Epub 2001 Nov 20. PMID:11717396

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