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The crystal structures of native hydroquinone 1,2-dioxygenase from Sphingomonas sp. TTNP3 and of substrate and inhibitor complexes.
Journal article

The crystal structures of native hydroquinone 1,2-dioxygenase from Sphingomonas sp. TTNP3 and of substrate and inhibitor complexes.

  • Ferraroni M Dipartimento di Chimica "Ugo Schiff", Università di Firenze, Via della Lastruccia 3, I-50019, Sesto Fiorentino, FI, Italy. Electronic address: marta.ferraroni@unifi.it.
  • Da Vela S Dipartimento di Chimica "Ugo Schiff", Università di Firenze, Via della Lastruccia 3, I-50019, Sesto Fiorentino, FI, Italy. Electronic address: stefanodavela@gmail.com.
  • Kolvenbach BA Institute for Ecopreneurship, School of Life Sciences, University of Applied Sciences and Arts Northwestern Switzerland, Gründenstrasse 40, 4132 Muttenz, Switzerland. Electronic address: boris.kolvenbach@fhnw.ch.
  • Corvini PFX Institute for Ecopreneurship, School of Life Sciences, University of Applied Sciences and Arts Northwestern Switzerland, Gründenstrasse 40, 4132 Muttenz, Switzerland. Electronic address: philippe.corvini@fhnw.ch.
  • Scozzafava A Dipartimento di Chimica "Ugo Schiff", Università di Firenze, Via della Lastruccia 3, I-50019, Sesto Fiorentino, FI, Italy. Electronic address: andrea.scozzafava@unifi.it.
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  • 2017-02-25
Published in:
  • Biochimica et biophysica acta. Proteins and proteomics. - 2017
Crystallography
Cupin superfamily
Dioxygenase
Metal binding motif
Ring cleaving
Amino Acid Sequence
Binding Sites
Catalytic Domain
Crystallography, X-Ray
Dioxygenases
Hydroquinones
Iron
Nitrophenols
Parabens
Protein Conformation
Sequence Homology, Amino Acid
Sphingomonas
English The crystal structure of hydroquinone 1,2-dioxygenase, a Fe(II) ring cleaving dioxygenase from Sphingomonas sp. strain TTNP3, which oxidizes a wide range of hydroquinones to the corresponding 4-hydroxymuconic semialdehydes, has been solved by Molecular Replacement, using the coordinates of PnpCD from Pseudomonas sp. strain WBC-3. The enzyme is a heterotetramer, constituted of two subunits α and two β of 19 and 38kDa, respectively. Both the two subunits fold as a cupin, but that of the small α subunit lacks a competent metal binding pocket. Two tetramers are present in the asymmetric unit. Each of the four β subunits in the asymmetric unit binds one Fe(II) ion. The iron ion in each β subunit is coordinated to three protein residues, His258, Glu264, and His305 and a water molecule. The crystal structures of the complexes with the substrate methylhydroquinone, obtained under anaerobic conditions, and with the inhibitors 4-hydroxybenzoate and 4-nitrophenol were also solved. The structures of the native enzyme and of the complexes present significant differences in the active site region compared to PnpCD, the other hydroquinone 1,2-dioxygenase of known structure, and in particular they show a different coordination at the metal center.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://folia.unifr.ch/global/documents/62601
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