1jmx
From Proteopedia
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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 NI and HEC 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
Page seeded by OCA on Tue Nov 20 18:23:23 2007
