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Please use this identifier to cite or link to this item: http://repository.iitr.ac.in/handle/123456789/1099
Title: Biochemical studies and ligand-bound structures of biphenyl dehydrogenase from pandoraea pnomenusa strain B-356 reveal a basis for broad specificity of the enzyme
Authors: Dhindwal S.
Patil D.N.
Mohammadi M.
Sylvestre M.
Tomar, Shailly
Kumar, Pravindra R.Manish
Published in: Journal of Biological Chemistry
Abstract: Biphenyl dehydrogenase, a member of short-chain dehydrogenase/ reductase enzymes, catalyzes the second step of the biphenyl/polychlorinated biphenyls catabolic pathway in bacteria. To understand the molecular basis for the broad substrate specificity of Pandoraea pnomenusa strain B-356 biphenyl dehydrogenase (BphB B-356), the crystal structures of the apoenzyme, the binary complex with NAD +, and the ternary complexes with NAD +-2,3-dihydroxybiphenyl and NAD +-4,4?- dihydroxybiphenyl were determined at 2.2-, 2.5-, 2.4-, and 2.1- Åresolutions, respectively. A crystal structure representing an intermediate state of the enzyme was also obtained in which the substrate binding loop was ordered as compared with the apo and binary forms but it was displaced significantly with respect to the ternary structures. These five structures reveal that the substrate binding loop is highly mobile and that its conformation changes during ligand binding, starting from a disorganized loop in the apo state to a well organized loop structure in the ligand-bound form. Conformational changes are induced during ligand binding; forming a well defined cavity to accommodate a wide variety of substrates. This explains the biochemical data that shows BphB B-356 converts the dihydrodiol metabolites of 3,3?-dichlorobiphenyl, 2,4,4?-trichlorobiphenyl, and 2,6-dichlorobiphenyl to their respective dihydroxy metabolites. For the first time, a combination of structural, biochemical, and molecular docking studies of BphB B-356 elucidate the unique ability of the enzyme to transform the cis-dihydrodiols of double meta-, para-, and ortho-substituted chlorobiphenyls. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
Citation: Journal of Biological Chemistry(2011), 286(42): 37011-37022
URI: https://doi.org/10.1074/jbc.M111.291013
http://repository.iitr.ac.in/handle/123456789/1099
Issue Date: 2011
ISSN: 219258
Author Scopus IDs: 36082537700
26431600400
23390544500
7005984229
57203506001
55064809000
Author Affiliations: Dhindwal, S., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667, India
Patil, D.N., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667, India
Mohammadi, M., I
Corresponding Author: Kumar, P.; Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667, India; email: pravshai@gmail.com
Appears in Collections:Journal Publications [BT]

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