Crystal structure of Quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thio-ether cross-bridges

doi:10.1074/jbc.M109090200

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Papers In Press, published online ahead of print November 9, 2001
J. Biol. Chem, 10.1074/jbc.M109090200
Submitted on September 20, 2001
Revised on October 26, 2001
Accepted on November 8, 2001

Crystal structure of Quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thio-ether cross-bridges

Atsuko Satoh, Jong-Keun Kim, Ikuko Miyahara, Bart Devreese, Isabel Vandenberghe, Ayse Hacisalihoglu, Toshihide Okajima, Shun’ichi Kuroda, Osao Adachi, Johannis A. Duine, Jozef Van Beeumen, Katsuyuki Tanizawa, and Ken Hirotsu

Department of Chemistry, Graduate School of Science, Osaka City University, Osaka 558-8585

Corresponding Author: hirotsu{at}sci.osaka-cu.ac.jp

The crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida has been determined at 1.9-Å resolution. The enzyme consists of three non-identical subunits; a four-domain $alpha$ -subunit that harbors a diheme 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 crosslinked, proteinous quinone cofactor, cysteine tryptophylquinone (CTQ). More surprisingly, the catalytic $gamma$ -subunit contains three additional crosslinks that encage the CTQ 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 unique containing four internal crosslinks in such a short polypeptide chain, which would otherwise be difficult to fold into a globular structure.

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