1jmz

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(New page: 200px<br /><applet load="1jmz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jmz, resolution 2.0&Aring;" /> '''crystal structure of ...)
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[[Image:1jmz.jpg|left|200px]]<br /><applet load="1jmz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jmz, resolution 2.0&Aring;" />
caption="1jmz, resolution 2.0&Aring;" />
'''crystal structure of a quinohemoprotein amine dehydrogenase from pseudomonas putida with inhibitor'''<br />
'''crystal structure of a quinohemoprotein amine dehydrogenase from pseudomonas putida with inhibitor'''<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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1JMZ 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, PND 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=1JMZ OCA].
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1JMZ 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>, <scene name='pdbligand=PND:'>PND</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=1JMZ 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 18:23:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:25 2008''

Revision as of 11:24, 21 February 2008

Image:1jmz.jpg

1jmz, resolution 2.0Å

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crystal structure of a quinohemoprotein amine dehydrogenase from pseudomonas putida with inhibitor

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

1JMZ 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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