RRC ID 29155
Author 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.
Title Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges.
Journal J. Biol. Chem.
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.
Volume 277(4)
Pages 2830-4
Published 2002-1-25
DOI 10.1074/jbc.M109090200
PII M109090200
PMID 11704672
MeSH Amino Acids / chemistry Aspartic Acid / chemistry Binding Sites Catalytic Domain Crystallography, X-Ray Cysteine / chemistry Dipeptides / biosynthesis Dipeptides / chemistry* Glutamic Acid / chemistry Indolequinones* Models, Molecular Oxidoreductases Acting on CH-NH Group Donors / chemistry* Protein Conformation Protein Folding Protein Structure, Tertiary Pseudomonas putida / enzymology* Quinones / chemistry* Sulfides / chemistry
IF 4.106
Times Cited 53
DNA material pUCP-Nde-QH-AmDH (RDB02849)