1jmx

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(New page: 200px<br /><applet load="1jmx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jmx, resolution 1.9&Aring;" /> '''crystal structure of ...)
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[[Image:1jmx.jpg|left|200px]]<br /><applet load="1jmx" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jmx, resolution 1.9&Aring;" />
caption="1jmx, resolution 1.9&Aring;" />
'''crystal structure of a quinohemoprotein amine dehydrogenase from pseudomonas putida'''<br />
'''crystal structure of a quinohemoprotein amine dehydrogenase from pseudomonas putida'''<br />
==Overview==
==Overview==
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The crystal structure of a quinohemoprotein amine dehydrogenase from, Pseudomonas putida has been determined at 1.9-A resolution. The enzyme, comprises three non-identical subunits: a four-domain alpha-subunit that, harbors a di-heme cytochrome c, a seven-bladed beta-propeller beta-subunit, that provides part of the active site, and a small gamma-subunit that, contains a novel cross-linked, proteinous quinone cofactor, cysteine, tryptophylquinone. More surprisingly, the catalytic gamma-subunit contains, three additional chemical cross-links that encage the cysteine, tryptophylquinone cofactor, involving a cysteine side chain bridged to, either an Asp or Glu residue all in a hitherto unknown thioether bonding, with a methylene carbon atom of acidic amino acid side chains. Thus, the, structure of the 79-residue gamma-subunit is quite unusual, containing, four internal cross-links in such a short polypeptide chain that would, otherwise be difficult to fold into a globular structure.
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The crystal structure of a quinohemoprotein amine dehydrogenase from Pseudomonas putida has been determined at 1.9-A resolution. The enzyme comprises three non-identical subunits: a four-domain alpha-subunit that harbors a di-heme cytochrome c, a seven-bladed beta-propeller beta-subunit that provides part of the active site, and a small gamma-subunit that contains a novel cross-linked, proteinous quinone cofactor, cysteine tryptophylquinone. More surprisingly, the catalytic gamma-subunit contains three additional chemical cross-links that encage the cysteine tryptophylquinone cofactor, involving a cysteine side chain bridged to either an Asp or Glu residue all in a hitherto unknown thioether bonding with a methylene carbon atom of acidic amino acid side chains. Thus, the structure of the 79-residue gamma-subunit is quite unusual, containing four internal cross-links in such a short polypeptide chain that would otherwise be difficult to fold into a globular structure.
==About this Structure==
==About this Structure==
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1JMX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with NI and HEC as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JMX OCA].
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1JMX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMX OCA].
==Reference==
==Reference==
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[[Category: amine dehydrogenase]]
[[Category: amine dehydrogenase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:23:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:24 2008''

Revision as of 11:24, 21 February 2008


1jmx, resolution 1.9Å

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crystal structure of a quinohemoprotein amine dehydrogenase from pseudomonas putida

Overview

The crystal structure of a quinohemoprotein amine dehydrogenase from Pseudomonas putida has been determined at 1.9-A resolution. The enzyme comprises three non-identical subunits: a four-domain alpha-subunit that harbors a di-heme cytochrome c, a seven-bladed beta-propeller beta-subunit that provides part of the active site, and a small gamma-subunit that contains a novel cross-linked, proteinous quinone cofactor, cysteine tryptophylquinone. More surprisingly, the catalytic gamma-subunit contains three additional chemical cross-links that encage the cysteine tryptophylquinone cofactor, involving a cysteine side chain bridged to either an Asp or Glu residue all in a hitherto unknown thioether bonding with a methylene carbon atom of acidic amino acid side chains. Thus, the structure of the 79-residue gamma-subunit is quite unusual, containing four internal cross-links in such a short polypeptide chain that would otherwise be difficult to fold into a globular structure.

About this Structure

1JMX is a Protein complex structure of sequences from Pseudomonas putida with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges., Satoh A, Kim JK, Miyahara I, Devreese B, Vandenberghe I, Hacisalihoglu A, Okajima T, Kuroda S, Adachi O, Duine JA, Van Beeumen J, Tanizawa K, Hirotsu K, J Biol Chem. 2002 Jan 25;277(4):2830-4. Epub 2001 Nov 9. PMID:11704672

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