1BDB

CIS-BIPHENYL-2,3-DIHYDRODIOL-2,3-DEHYDROGENASE FROM PSEUDOMONAS SP. LB400

Summary for 1BDB

• Entry DOI: 10.2210/pdb1bdb/pdb
• Descriptor: CIS-BIPHENYL-2,3-DIHYDRODIOL-2,3-DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: nad-dependent oxidoreductase, short-chain alcohol dehydrogenase, pcb degradation, oxidoreductase
• Biological source: Pseudomonas sp.
• Total number of polymer chains: 1
• Total formula weight: 29593.29

Authors

Huelsmeyer, M.,Hecht, H.-J.,Niefind, K.,Hofer, B.,Timmis, K.N.,Schomburg, D. (deposition date: 1997-05-10, release date: 1997-11-12, Last modification date: 2024-05-22)

Primary citation

Hulsmeyer, M.,Hecht, H.J.,Niefind, K.,Hofer, B.,Eltis, L.D.,Timmis, K.N.,Schomburg, D.
Crystal structure of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from a PCB degrader at 2.0 A resolution.
Protein Sci., 7:1286-1293, 1998

PubMed Abstract: 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.

PubMed: 9655331

Experimental method

X-RAY DIFFRACTION (2 Å)