論文 - 詳細
RRC ID | 29156 |
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著者 | Datta S, Mori Y, Takagi K, Kawaguchi K, Chen ZW, Okajima T, Kuroda S, Ikeda T, Kano K, Tanizawa K, Mathews FS. |
タイトル | Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking. |
ジャーナル | Proc Natl Acad Sci U S A |
Abstract |
The crystal structure of the heterotrimeric quinohemoprotein amine dehydrogenase from Paracoccus denitrificans has been determined at 2.05-A resolution. Within an 82-residue subunit is contained an unusual redox cofactor, cysteine tryptophylquinone (CTQ), consisting of an orthoquinone-modified tryptophan side chain covalently linked to a nearby cysteine side chain. The subunit is surrounded on three sides by a 489-residue, four-domain subunit that includes a diheme cytochrome c. Both subunits sit on the surface of a third subunit, a 337-residue seven-bladed beta-propeller that forms part of the enzyme active site. The small catalytic subunit is internally crosslinked by three highly unusual covalent cysteine to aspartic or glutamic acid thioether linkages in addition to the cofactor crossbridge. The catalytic function of the enzyme as well as the biosynthesis of the unusual catalytic subunit is discussed. |
巻・号 | 98(25) |
ページ | 14268-73 |
公開日 | 2001-12-4 |
DOI | 10.1073/pnas.241429098 |
PII | 241429098 |
PMID | 11717396 |
PMC | PMC64671 |
MeSH | Amino Acid Sequence Catalytic Domain Coenzymes / biosynthesis Coenzymes / chemistry Cross-Linking Reagents Crystallography, X-Ray Models, Molecular Molecular Sequence Data Molecular Structure Oxidation-Reduction Oxidoreductases Acting on CH-NH Group Donors / biosynthesis Oxidoreductases Acting on CH-NH Group Donors / chemistry* Oxidoreductases Acting on CH-NH Group Donors / genetics Paracoccus denitrificans / enzymology* Paracoccus denitrificans / genetics Protein Structure, Quaternary Protein Subunits Sequence Homology, Amino Acid |
IF | 9.412 |
引用数 | 113 |
WOS 分野 | BIOCHEMISTRY & MOLECULAR BIOLOGY |
リソース情報 | |
遺伝子材料 | pET-36-QHNDH (RDB02848) |