Structures of an extradiol catechol dioxygenase – C23O64, from 3-nitrotoluene degrading Diaphorobacter sp. strain DS2 in substrate-free, substrate-bound and substrate analog-bound states

This manuscript reports structure–function studies of Catechol 2,3-dioxygenase ( C23O64 ), which is the second enzyme in the metabolic degradation pathway of 3-nitrotoluene by Diaphorobacter sp. strain DS2. The recombinant protein is a ring cleavage enzyme for 3-methylcatechol and 4-methylcatechol p...

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Published in:Experimental Results 2020-01, Vol.1, Article e48
Main Authors: Mishra, Keerti, Arya, Chetan Kumar, Subramanian, Ramaswamy, Ramanathan, Gurunath
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Language:English
Subjects:
Amino acids
aromatic ring cleavage
Catechol 2,3-dioxygenase
Diaphorobacter sp. strain DS2
Enzymes
extradiol dioxygenases
Geometry
Ligands
Mononuclear iron-containing enzymes
Proteins
Scholarships & fellowships
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Subramanian, Ramaswamy
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description This manuscript reports structure–function studies of Catechol 2,3-dioxygenase ( C23O64 ), which is the second enzyme in the metabolic degradation pathway of 3-nitrotoluene by Diaphorobacter sp. strain DS2. The recombinant protein is a ring cleavage enzyme for 3-methylcatechol and 4-methylcatechol products formed after dioxygenation of the aromatic ring. Here we report the substrate-free, substrate-bound, and substrate-analog bound crystal structures of C23O64. The protein crystallizes in the P6(2)22 space-group. The structures were determined by molecular replacement and refined to resolutions of 2.4, 2.4, 2.2 Å, respectively. A comparison of the structures with related extradiol dioxygenases showed 22 conserved residues. A comparison of the active site pocket with catechol 2,3-dioxygenase ( LapB) from Pseudomonas sp KL28 and homoprotocatechuate 2,3-dioxygenase (HPCD) from Brevibacterium fuscum shows significant similarities to suggest that the mechanism of enzyme action is similar to HPCD .
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A comparison of the active site pocket with catechol 2,3-dioxygenase ( LapB) from Pseudomonas sp KL28 and homoprotocatechuate 2,3-dioxygenase (HPCD) from Brevibacterium fuscum shows significant similarities to suggest that the mechanism of enzyme action is similar to HPCD .</description><identifier>ISSN: 2516-712X</identifier><identifier>EISSN: 2516-712X</identifier><identifier>DOI: 10.1017/exp.2020.50</identifier><language>eng</language><publisher>Cambridge: Cambridge University Press</publisher><subject>Amino acids ; aromatic ring cleavage ; Catechol 2,3-dioxygenase ; Diaphorobacter sp. strain DS2 ; Enzymes ; extradiol dioxygenases ; Geometry ; Ligands ; Mononuclear iron-containing enzymes ; Proteins ; Scholarships &amp; fellowships</subject><ispartof>Experimental Results, 2020-01, Vol.1, Article e48</ispartof><rights>The Author(s), 2020. Published by Cambridge University Press. 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subjects Amino acids
aromatic ring cleavage
Catechol 2,3-dioxygenase
Diaphorobacter sp. strain DS2
Enzymes
extradiol dioxygenases
Geometry
Ligands
Mononuclear iron-containing enzymes
Proteins
Scholarships & fellowships
title Structures of an extradiol catechol dioxygenase – C23O64, from 3-nitrotoluene degrading Diaphorobacter sp. strain DS2 in substrate-free, substrate-bound and substrate analog-bound states
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