Roberto A Steiner

Summary

Affiliation: King's College London
Country: UK

Publications

  1. doi request reprint Origin of the Proton-transfer Step in the Cofactor-free (1H)-3-Hydroxy-4-oxoquinaldine 2,4-Dioxygenase: EFFECT OF THE BASICITY OF AN ACTIVE SITE HIS RESIDUE
    Aitor Hernández-Ortega
    From the Manchester Institute of Biotechnology, University of Manchester, Manchester M1 7DN and
    J Biol Chem 289:8620-32. 2014
  2. pmc Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold
    Roberto A Steiner
    Randall Division of Cell and Molecular Biophysics, King s College London, New Hunt s House, Guy s Campus, London SE1 1UL, England
    Proc Natl Acad Sci U S A 107:657-62. 2010
  3. pmc Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rü61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily
    Roberto A Steiner
    Randall Division of Cell and Molecular Biophysics, King s College London, New Hunt s House, Guy s Campus, London SE1 1UL, England
    Acta Crystallogr Sect F Struct Biol Cryst Commun 63:382-5. 2007
  4. pmc Structural insight into M-band assembly and mechanics from the titin-obscurin-like-1 complex
    Stefano Pernigo
    King s College London BHF Research Excellence Centre, Randall Division for Cell and Molecular Biophysics and Cardiovascular Division, New Hunt s House, Guy s Campus, London SE1 1UL, United Kingdom
    Proc Natl Acad Sci U S A 107:2908-13. 2010
  5. ncbi request reprint Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. Ligand-induced coordination changes probed by X-ray crystallography: inhibition, ordering effect, and mechanistic insights
    Roberto A Steiner
    Laboratory of Biophysical Chemistry, Department of Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
    Biochemistry 41:7955-62. 2002
  6. ncbi request reprint REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use
    Alexei A Vagin
    Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, England
    Acta Crystallogr D Biol Crystallogr 60:2184-95. 2004
  7. ncbi request reprint DNA variability in five crystal structures of d(CGCAATTGCG)
    Núria Valls
    Departament d Enginyeria Quimica, Universitat Politecnica de Catalunya, Avinguda Diagonal 647, E 08028 Barcelona, Spain
    Acta Crystallogr D Biol Crystallogr 60:680-5. 2004
  8. ncbi request reprint Fisher's information in maximum-likelihood macromolecular crystallographic refinement
    Roberto A Steiner
    Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, England
    Acta Crystallogr D Biol Crystallogr 59:2114-24. 2003
  9. pmc Single-crystal EPR study at 95 GHz of the type 2 copper site of the inhibitor-bound quercetin 2,3-dioxygenase
    Maria Fittipaldi
    Department of Molecular Physics, Huygens Laboratory, Leiden University, Leiden, The Netherlands
    Biophys J 85:4047-54. 2003
  10. pmc Anaerobic enzyme.substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase
    Roberto A Steiner
    Laboratory of Biophysical Chemistry, Department of Chemistry, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands
    Proc Natl Acad Sci U S A 99:16625-30. 2002

Collaborators

  • Susanne Fetzner
  • Aaron J Oakley
  • Andrey A Lebedev
  • Aitor Hernández-Ortega
  • Stefano Pernigo
  • Bauke W Dijkstra
  • Alexei A Vagin
  • Núria Valls
  • Garib N Murshudov
  • Maria Fittipaldi
  • Martina Huber
  • Derren J Heyes
  • Paula I van Noort
  • Dominic P H M Heuts
  • Sam P de Visser
  • Maarten R Egmond
  • Soi Bui
  • Matthew G Quesne
  • Fabrizia Fusetti
  • Ingeborg M Kooter
  • Nigel S Scrutton
  • Morten Bertz
  • Matthias Rief
  • Mathias Gautel
  • Atsushi Fukuzawa
  • Mark Holt
  • Glenford Wright
  • Liz Potterton
  • Fei Long
  • Stuart McNicholas
  • Juan A Subirana
  • Edgar J J Groenen
  • Michio Matsushita
  • Klaus H Schröter
  • Tjaard Pijning
  • Kor H Kalk
  • Henriette J Rozeboom

Detail Information

Publications14

  1. doi request reprint Origin of the Proton-transfer Step in the Cofactor-free (1H)-3-Hydroxy-4-oxoquinaldine 2,4-Dioxygenase: EFFECT OF THE BASICITY OF AN ACTIVE SITE HIS RESIDUE
    Aitor Hernández-Ortega
    From the Manchester Institute of Biotechnology, University of Manchester, Manchester M1 7DN and
    J Biol Chem 289:8620-32. 2014
    ..This multidisciplinary study offers unambiguous support to the view that substrate deprotonation, driven by the His/Asp dyad, is an essential requirement for its activation. ..
  2. pmc Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold
    Roberto A Steiner
    Randall Division of Cell and Molecular Biophysics, King s College London, New Hunt s House, Guy s Campus, London SE1 1UL, England
    Proc Natl Acad Sci U S A 107:657-62. 2010
    ..Our analysis provides a framework to explain cofactor-independent dioxygenation within a protein architecture generally employed to catalyze hydrolytic reactions...
  3. pmc Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rü61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily
    Roberto A Steiner
    Randall Division of Cell and Molecular Biophysics, King s College London, New Hunt s House, Guy s Campus, London SE1 1UL, England
    Acta Crystallogr Sect F Struct Biol Cryst Commun 63:382-5. 2007
    ..5 A resolution at the Cu absorption peak wavelength. The crystals belong to the primitive tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 153.788, c = 120.872 A...
  4. pmc Structural insight into M-band assembly and mechanics from the titin-obscurin-like-1 complex
    Stefano Pernigo
    King s College London BHF Research Excellence Centre, Randall Division for Cell and Molecular Biophysics and Cardiovascular Division, New Hunt s House, Guy s Campus, London SE1 1UL, United Kingdom
    Proc Natl Acad Sci U S A 107:2908-13. 2010
    ....
  5. ncbi request reprint Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. Ligand-induced coordination changes probed by X-ray crystallography: inhibition, ordering effect, and mechanistic insights
    Roberto A Steiner
    Laboratory of Biophysical Chemistry, Department of Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
    Biochemistry 41:7955-62. 2002
    ..Compared to the native coordinating conformation, this conformation is approximately 90 degrees rotated about the chi(3) angle. This latter Glu73 conformation is compatible with the presence of a bound substrate...
  6. ncbi request reprint REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use
    Alexei A Vagin
    Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, England
    Acta Crystallogr D Biol Crystallogr 60:2184-95. 2004
    ..In many cases, the REFMAC5 dictionary allows entirely automatic generation of restraints within REFMAC5 refinement runs...
  7. ncbi request reprint DNA variability in five crystal structures of d(CGCAATTGCG)
    Núria Valls
    Departament d Enginyeria Quimica, Universitat Politecnica de Catalunya, Avinguda Diagonal 647, E 08028 Barcelona, Spain
    Acta Crystallogr D Biol Crystallogr 60:680-5. 2004
    ..As a result of the higher resolution of the crystal structure, a more regular structure was obtained and a clear definition of the spine of hydration was observed which was not visible in the four previous structures...
  8. ncbi request reprint Fisher's information in maximum-likelihood macromolecular crystallographic refinement
    Roberto A Steiner
    Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, England
    Acta Crystallogr D Biol Crystallogr 59:2114-24. 2003
    ..The scoring algorithm has been implemented in the program REFMAC5 of the CCP4 suite. The Fisher's matrix is used in its sparse approximation. Tests indicate that the algorithm performs satisfactorily...
  9. pmc Single-crystal EPR study at 95 GHz of the type 2 copper site of the inhibitor-bound quercetin 2,3-dioxygenase
    Maria Fittipaldi
    Department of Molecular Physics, Huygens Laboratory, Leiden University, Leiden, The Netherlands
    Biophys J 85:4047-54. 2003
    ..The orientation of the g-tensor for the quercetin 2,3-dioxygenase is compared with that for type 1 copper sites...
  10. pmc Anaerobic enzyme.substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase
    Roberto A Steiner
    Laboratory of Biophysical Chemistry, Department of Chemistry, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands
    Proc Natl Acad Sci U S A 99:16625-30. 2002
    ..Structure-based geometric considerations indicate O(2) binding to the flavonol C2 atom as the preferred route for flavonol dioxygenation...
  11. ncbi request reprint EPR characterization of the mononuclear Cu-containing Aspergillus japonicus quercetin 2,3-dioxygenase reveals dramatic changes upon anaerobic binding of substrates
    Ingeborg M Kooter
    Unilever Research Vlaardingen, The Netherlands
    Eur J Biochem 269:2971-9. 2002
    ..Several differences are noted between A. japonicus 2,3QD and the enzyme from A. niger German Collection of Microorganisms 821...
  12. ncbi request reprint Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 2. X-ray absorption studies of native enzyme and anaerobic complexes with the substrates quercetin and myricetin
    Roberto A Steiner
    Laboratory of Biophysical Chemistry, Department of Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
    Biochemistry 41:7963-8. 2002
    ..In addition, monodentate carboxylate ligation by the Glu73 side chain is likely to play a role in the fine-tuning of the equilibrium leading to the formation of the activated E.S complex...
  13. ncbi request reprint Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus
    Fabrizia Fusetti
    Laboratory of Biophysical Chemistry, Department of Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
    Structure 10:259-68. 2002
    ..Manual docking of the substrate quercetin into the active site showed that the different geometries of the copper site might be of catalytic importance...