1bdb: Difference between revisions

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==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 mechanism, is proposed for cis-dihydrodiol dehydrogenases.

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==

Line 13:

[[Category: Pseudomonas sp.]]

[[Category: Single protein]]

[[Category: Hecht, H.J.]]

[[Category: Hecht, H J.]]

[[Category: Hofer, B.]]

[[Category: Huelsmeyer, M.]]

[[Category: Niefind, K.]]

[[Category: Schomburg, D.]]

[[Category: Timmis, K.N.]]

[[Category: Timmis, K N.]]

[[Category: NAD]]

[[Category: nad-dependent oxidoreductase]]

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[[Category: short-chain alcohol dehydrogenase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:03 2008''

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@@ Line 4: / Line 4: @@
 ==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 mechanism, is proposed for cis-dihydrodiol dehydrogenases.
+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==
@@ Line 13: / Line 13: @@
 [[Category: Pseudomonas sp.]]
 [[Category: Single protein]]
-[[Category: Hecht, H.J.]]
+[[Category: Hecht, H J.]]
 [[Category: Hofer, B.]]
 [[Category: Huelsmeyer, M.]]
 [[Category: Niefind, K.]]
 [[Category: Schomburg, D.]]
-[[Category: Timmis, K.N.]]
+[[Category: Timmis, K N.]]
 [[Category: NAD]]
 [[Category: nad-dependent oxidoreductase]]
@@ Line 24: / Line 24: @@
 [[Category: short-chain alcohol dehydrogenase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:32:39 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:03 2008''