1JMX
crystal structure of a quinohemoprotein amine dehydrogenase from pseudomonas putida
Summary for 1JMX
Entry DOI | 10.2210/pdb1jmx/pdb |
Related | 1JMZ |
Descriptor | Amine Dehydrogenase, NICKEL (II) ION, HEME C, ... (6 entities in total) |
Functional Keywords | amine dehydrogenase, oxidoreductase |
Biological source | Pseudomonas putida More |
Cellular location | Periplasm: P0A182 |
Total number of polymer chains | 3 |
Total formula weight | 103197.57 |
Authors | Satoh, A.,Miyahara, I.,Hirotsu, K. (deposition date: 2001-07-20, release date: 2002-01-16, Last modification date: 2011-07-13) |
Primary citation | Satoh, A.,Kim, J.K.,Miyahara, I.,Devreese, B.,Vandenberghe, I.,Hacisalihoglu, A.,Okajima, T.,Kuroda, S.,Adachi, O.,Duine, J.A.,Van Beeumen, J.,Tanizawa, K.,Hirotsu, K. Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges. J.Biol.Chem., 277:2830-2834, 2002 Cited by PubMed Abstract: 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. PubMed: 11704672DOI: 10.1074/jbc.M109090200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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