5xbp

Oxygenase component of 3-nitrotoluene dioxygenase from Diaphorobacter sp. strain DS2

spinqualitylabelsall models 5xbp, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xbp is a 6 chain structure with sequence from Diaphorobacter sp. DS2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: FE, FES Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M9PW10_9BURK Publication Abstract from PubMed 3-nitrotoluene dioxygenase (3NTDO) from Diaphorobacter sp. strain DS2 catalyses the conversion of 3-nitrotoluene (3NT) into a mixture of 3- and 4-methylcatechols with release of nitrite. We report here, X-ray crystal structures of oxygenase and ferredoxin components of 3NTDO at 2.9 A and 2.4 A, respectively. The residues responsible for nitrite release in 3NTDO were further probed by four single and two double mutations in the catalytic site of alpha-subunit of the dioxygenase. Modification of Val 350 to Phe, Ile 204 to Ala, and Asn258 to Val by site directed mutagenesis resulted in inactive enzymes revealing the importance of these residues in catalysis. Docking studies of meta nitrotoluene to the active site of 3NTDO suggested possible orientations of binding that favor the formation of 3-methylcatechol (3MC) over 4-methylcatechol energetically. The electron transfer pathway from ferredoxin subunit to the active site of the oxygenase subunit is also proposed. Structural and functional studies of ferredoxin and oxygenase components of 3-nitrotoluene dioxygenase from Diaphorobacter sp. strain DS2.,Kumari A, Singh D, Ramaswamy S, Ramanathan G PLoS One. 2017 Apr 27;12(4):e0176398. doi: 10.1371/journal.pone.0176398., eCollection 2017. PMID:28448625 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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