Citrobacter koseri ATCC BAA-895

Summary

Alias: Citrobacter (diversus) koseri ATCC BAA-895, Citrobacter koseri str. ATCC BAA-895, Citrobacter koseri strain ATCC BAA-895

Top Publications

  1. pmc 3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle
    Justin Chartron
    Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA
    Biochemistry 46:3942-51. 2007
  2. pmc Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions
    Dalibor Milić
    Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, HR 10000 Zagreb, Croatia
    Biochemistry 45:7544-52. 2006
  3. ncbi Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding
    M Eriksson
    Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, Sweden
    Structure 5:1077-92. 1997
  4. pmc Structure of Citrobacter freundii L-methionine gamma-lyase
    D V Mamaeva
    Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str 32, 119991 Moscow, Russia
    Acta Crystallogr Sect F Struct Biol Cryst Commun 61:546-9. 2005
  5. ncbi A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase
    A L Persson
    Department of Molecular Biology, Stockholm University, Stockholm, Sweden
    J Biol Chem 272:31533-41. 1997
  6. ncbi Three-dimensional structure of tyrosine phenol-lyase
    A A Antson
    Shubnikov Institute of Crystallography, Russian Academy of Sciences, Moscow
    Biochemistry 32:4195-206. 1993
  7. ncbi QnrB9 in association with TEM-116 extended-spectrum beta-lactamase in Citrobacter freundii isolated from sewage effluent: first report from Italy
    C Forcella
    Dipartimento di Scienze e Tecnologie Biomediche, University of L Aquila, Italy
    J Chemother 22:243-5. 2010
  8. ncbi NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains
    Edvards Liepinsh
    Department of Medical Biochemistry, Karolinska Institute, S 17177 Stockholm, Sweden
    J Mol Biol 327:833-42. 2003
  9. ncbi The catalytic mechanism of tyrosine phenol-lyase from Erwinia herbicola: the effect of substrate structure on pH-dependence of kinetic parameters in the reactions with ring-substituted tyrosines
    N G Faleev
    Institue of Food Substances, Russian Academy of Sciences, Moscow, Russia
    Z Naturforsch C 51:363-70. 1996
  10. ncbi Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase
    C W Levy
    Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, United Kingdom
    Structure 10:105-13. 2002

Scientific Experts

  • C Forcella
  • Justin Chartron
  • T V Demidkina
  • Dalibor Milić
  • D V Mamaeva
  • Edvards Liepinsh
  • C W Levy
  • M Eriksson
  • G Celenza
  • M Perilli
  • M M Tavio
  • R Calabrese
  • C Pellegrini
  • G Amicosante
  • B Segatore
  • A A Antson
  • C David Stout
  • Carrie Shiau
  • Kate S Carroll
  • Dubravka Matković-Čalogović
  • R S Phillips
  • Tatyana V Demidkina
  • Nina I Sinitzina
  • Vitalia V Kulikova
  • Alfred A Antson
  • S V Revtovich
  • A D Nikulin
  • U Uhlin
  • S V Nikonov
  • E A Morozova
  • M B Garber
  • A L Persson
  • B M Sjoberg
  • B Sundararaju
  • Dominique Dehareng
  • Catherine Généreux
  • Bernard Joris
  • Gottfried Otting
  • P A Buckley
  • Y Asano
  • P J Baker
  • D W Rice
  • K S Wilson
  • Y Kato
  • S Sedelnikova
  • N G Faleev
  • H Eklund
  • P Gollnick
  • M Ekberg
  • M V Barbolina
  • S Ramaswamy
  • K Regnstrom
  • S Pötsch
  • G G Dodson
  • M Sahlin
  • B Katterle
  • V S Ivoilov
  • S N Spirina
  • E H Harutyunyan
  • Z Dauter
  • S N Berezhnoy
  • J Long
  • R L Von Tersch
  • D G Vassylyev
  • B V Strokopytov
  • H Terry
  • G N Murshudov
  • M N Isupov

Detail Information

Publications13

  1. pmc 3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle
    Justin Chartron
    Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA
    Biochemistry 46:3942-51. 2007
    ....
  2. pmc Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions
    Dalibor Milić
    Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, HR 10000 Zagreb, Croatia
    Biochemistry 45:7544-52. 2006
    ..Finally, the closed conformation allows us to model keto(imino)quinonoid, the key transition intermediate...
  3. ncbi Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding
    M Eriksson
    Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, Sweden
    Structure 5:1077-92. 1997
    ..Our aim has been to crystallographically demonstrate substrate binding and to locate the two effector-binding sites...
  4. pmc Structure of Citrobacter freundii L-methionine gamma-lyase
    D V Mamaeva
    Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str 32, 119991 Moscow, Russia
    Acta Crystallogr Sect F Struct Biol Cryst Commun 61:546-9. 2005
    ..The comparison of these structures revealed that there are differences in PLP-binding residues and positioning of the surrounding flexible loops...
  5. ncbi A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase
    A L Persson
    Department of Molecular Biology, Stockholm University, Stockholm, Sweden
    J Biol Chem 272:31533-41. 1997
    ....
  6. ncbi Three-dimensional structure of tyrosine phenol-lyase
    A A Antson
    Shubnikov Institute of Crystallography, Russian Academy of Sciences, Moscow
    Biochemistry 32:4195-206. 1993
    ....
  7. ncbi QnrB9 in association with TEM-116 extended-spectrum beta-lactamase in Citrobacter freundii isolated from sewage effluent: first report from Italy
    C Forcella
    Dipartimento di Scienze e Tecnologie Biomediche, University of L Aquila, Italy
    J Chemother 22:243-5. 2010
    ..This is the first finding in Italy of qnrB9 and TEM-116 in a non-clinical or animal strain...
  8. ncbi NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains
    Edvards Liepinsh
    Department of Medical Biochemistry, Karolinska Institute, S 17177 Stockholm, Sweden
    J Mol Biol 327:833-42. 2003
    ..This hypothesis is supported by the observation that human serum N-acetylmuramyl-L-alanine amidase seems to be identical with a soluble form of human PGRP-L...
  9. ncbi The catalytic mechanism of tyrosine phenol-lyase from Erwinia herbicola: the effect of substrate structure on pH-dependence of kinetic parameters in the reactions with ring-substituted tyrosines
    N G Faleev
    Institue of Food Substances, Russian Academy of Sciences, Moscow, Russia
    Z Naturforsch C 51:363-70. 1996
    ..The activity of Citrobacter enzyme towards DOPA is considerably less than that of E. herbicola enzyme, and its maximal value is attained at higher pH...
  10. ncbi Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase
    C W Levy
    Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, United Kingdom
    Structure 10:105-13. 2002
    ..This analysis resolves the conflict that had linked MAL to the histidine and phenylalanine ammonia lyase family of enzymes...
  11. ncbi The polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5'-phosphate-dependent enzyme
    A A Antson
    European Molecular Biology Laboratory, DESY, Hamburg, Germany
    FEBS Lett 302:256-60. 1992
    ..Each subunit consists of two domains. The topology of the large domain appears to be similar to that of the aminotransferases...
  12. ncbi The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity
    B Sundararaju
    Department of Chemistry, Center for Metalloenzyme Studies, University of Georgia, Athens 30602, USA
    Biochemistry 36:6502-10. 1997
    ..M., & Phillips. R. S. (1988) Biochemistry 27, 7333-7338], and hence Arg 381 is at least partially responsible for the substrate specificity of TPL...
  13. ncbi Structure of ribonucleotide reductase protein R1
    U Uhlin
    Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala
    Nature 370:533-9. 1994
    ..The fifth cysteine, in a loop in the centre of the barrel, is positioned to initiate the radical reaction...