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J. Biol. Chem., Vol. 277, Issue 4, 2830-2834, January 25, 2002
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From the The crystal structure of a quinohemoprotein amine
dehydrogenase from Pseudomonas putida has been determined
at 1.9-Å resolution. The enzyme comprises three non-identical
subunits: a four-domain The atomic coordinates and the structure factors (code 1JMX and 1JMZ) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
Crystal Structure of Quinohemoprotein Amine Dehydrogenase
from Pseudomonas putida
IDENTIFICATION OF A NOVEL QUINONE COFACTOR ENCAGED BY MULTIPLE
THIOETHER CROSS-BRIDGES*
,
,
,
,
, and
§§
Department of Chemistry, Graduate School of
Science, Osaka City University, Osaka 558-8585, Japan,
§ Department of Structural Molecular Biology, Institute of
Scientific and Industrial Research, Osaka University, Ibaraki, Osaka
567-0047, Japan, ¶ Laboratory of Protein Biochemistry and Protein
Engineering, University of Ghent, 9000 Ghent, Belgium,
Department of Microbiology and Enzymology, Delft University of
Technology, 2628 BC Delft, The Netherlands, and ** Department
of Biological Chemistry, Faculty of Agriculture, Yamaguchi University,
Yamaguchi 753-8515, Japan
-subunit that harbors a di-heme cytochrome
c, a seven-bladed
-propeller
-subunit that provides
part of the active site, and a small
-subunit that contains a novel
cross-linked, proteinous quinone cofactor, cysteine
tryptophylquinone. More surprisingly, the catalytic
-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
-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.
*
This study was supported by research grants from Japan
Society for the Promotion of Science (Priority Area to K. H., Category B to K. T. and to O. A., "Research for the Future" to K. H. and to K. T., "Bilateral Program" to O. A., and an Osaka University Center of Excellence (COE) program "Creation of Highly Harmonized Functional Materials" to K. T.) and by the Fund for Scientific Research-Flanders (to J. V. B. and to B. D.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.

To whom correspondence may be addressed. Tel: 81-6-6879-8460;
Fax: 81-6879-8464; E-mail: tanizawa@sanken.osaka-u.ac.jp.
§§
To whom correspondence may be addressed. Tel: 81-6-6605-2507;
Fax: 81-6605-3131; E-mail:
hirotsu@sci.osaka-cu.ac.jp.
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