1bdb: Difference between revisions
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==Overview== | ==Overview== | ||
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 . | 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. | ||
==About this Structure== | ==About this Structure== | ||
1BDB is a | 1BDB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: CAT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BDB OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: short-chain alcohol dehydrogenase]] | [[Category: short-chain alcohol dehydrogenase]] | ||
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Revision as of 14:12, 5 November 2007
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CIS-BIPHENYL-2,3-DIHYDRODIOL-2,3-DEHYDROGENASE FROM PSEUDOMONAS SP. LB400
OverviewOverview
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.
About this StructureAbout this Structure
1BDB is a Single protein structure of sequence from Pseudomonas sp. with NAD as ligand. Structure known Active Site: CAT. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from a PCB degrader at 2.0 A resolution., Hulsmeyer M, Hecht HJ, Niefind K, Hofer B, Eltis LD, Timmis KN, Schomburg D, Protein Sci. 1998 Jun;7(6):1286-93. PMID:9655331
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