RRC ID 29155
著者 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.
タイトル Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges.
ジャーナル 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.
巻・号 277(4)
ページ 2830-4
公開日 2002-1-25
DOI 10.1074/jbc.M109090200
PII S0021-9258(20)87738-2
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 4.238
引用数 68
WOS 分野 BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
遺伝子材料 pUCP-Nde-QH-AmDH (RDB02849)