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Crystal structure of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from a PCB degrader at 2.0 A resolution.
Hülsmeyer, M; Hecht, H J; Niefind, K; Hofer, B; Eltis, L D; Timmis, K N; Schomburg, D.
Afiliação
  • Hülsmeyer M; National Institute for Biotechnological Research (GBF), Department of Structure Research, Braunschweig, Germany.
Protein Sci ; 7(6): 1286-93, 1998 Jun.
Article em En | MEDLINE | ID: mdl-9655331
cis-Biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is involved in the aerobic biodegradation of polychlorinated biphenyls (PCBs). The crystal structure of the NAD+-enzyme complex was determined by molecular replacement and refined to an R-value of 17.9% at 2.0 A. As a member of the short-chain alcohol dehydrogenase/reductase (SDR) family, the overall protein fold and positioning of the catalytic triad in BphB are very similar to those observed in other SDR enzymes, although small differences occur in the cofactor binding site. Modeling studies indicate that the substrate is bound in a deep hydrophobic cleft close to the nicotinamide moiety of the NAD+ cofactor. These studies further suggest that Asn143 is a key determinant of substrate specificity. A two-step reaction mechanism is proposed for cis-dihydrodiol dehydrogenases.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oxirredutases / Bifenilos Policlorados Idioma: En Revista: Protein Sci Assunto da revista: BIOQUIMICA Ano de publicação: 1998 Tipo de documento: Article País de afiliação: Alemanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oxirredutases / Bifenilos Policlorados Idioma: En Revista: Protein Sci Assunto da revista: BIOQUIMICA Ano de publicação: 1998 Tipo de documento: Article País de afiliação: Alemanha