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) |