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1JMX

crystal structure of a quinohemoprotein amine dehydrogenase from pseudomonas putida

Summary for 1JMX
Entry DOI10.2210/pdb1jmx/pdb
Related1JMZ
DescriptorAmine Dehydrogenase, NICKEL (II) ION, HEME C, ... (6 entities in total)
Functional Keywordsamine dehydrogenase, oxidoreductase
Biological sourcePseudomonas putida
More
Cellular locationPeriplasm: P0A182
Total number of polymer chains3
Total formula weight103197.57
Authors
Satoh, A.,Miyahara, I.,Hirotsu, K. (deposition date: 2001-07-20, release date: 2002-01-16, Last modification date: 2011-07-13)
Primary citationSatoh, 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: 11704672
DOI: 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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數據於2024-11-13公開中

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