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Biochemistry of Vitamin B6 and PQQ pp 183–185Cite as

X-ray study of tryptophanase at 2.1 Å resolution

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Part of the book series: Advances in Life Sciences ((ALS))

Summary

Holotryptophanase from Proteus vulgaris was crystallized in the presence of K+. The structure was solved at 2.1 Å resolution by molecular replacement technique and refined to descrepancy factor R=15.6%. Each subunit of the tetramer consists of a large and a small domain. The folding of the PLP-binding domain is similar to that of sonic PLP-dependent enzymes. PLP-binding site is formed by two subunits. Potassium ions (one per subunit) arc localized in the interior between two subunits of “cataltical” dimer.

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References

  • Antson, A.A., Demidkina. T.V., Gollnick, P.. Dautcr. Z. Von Tersch. R.L.. Long. J.. Berezhnoy. S.N.. Phillips, R.S., Harutyunyan, E.H. & Wilson, K.S. (1993). Three-dimensional structure of tyrosine phenollyase. Biochemistry 32: 4195–4206.

    Google Scholar 

  • Kamath. A.V. & Yanofsky. C. (1992). Characterization of the tryptophanase operon of Proteus vulgari.s. Cloning, nucleotide sequence, aminoacid homology and ìn vitro synthesis of the leader peptide and regulatory analysis. J.Biol.Chem. 267: 19978–19985.

    PubMed  CAS  Google Scholar 

  • Navata. J. (1992). AMoRe: A new package for molecular replacement. In: Proc of the CCP4Study Weekend. SERC Daresbury Laboratory. U.K., pp. 87–90.

    Google Scholar 

  • Snell. E.E. (1975). Tryptophanase: structure. catalytic activities. and mechanism of action. Advan. Enzeneol. 42: 287–333.

    Google Scholar 

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Author information

Authors and Affiliations

  1. Shubnikov Institute of Crystallography, Moscow, Russia

    M. Isupov & E. G. Harutyunyan

  2. Engelhardt Institute of Molecular Biology, Moscow, Russia

    I. Dementieva & L. Zakomirdina

  3. EMBL, Hamburg, Germany

    K. S. Wilson & Z. Dauter

  4. Dept. of Chemistry, University of York, York, England

    A. A. Antson & G. G. Dodson

Authors
  1. M. Isupov
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  2. I. Dementieva
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  3. L. Zakomirdina
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  4. K. S. Wilson
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  5. Z. Dauter
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  6. A. A. Antson
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  7. G. G. Dodson
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  8. E. G. Harutyunyan
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Editor information

Editors and Affiliations

  1. Dipartimento di Chimica Organica e Biologica, Università di Napoli “Federico II”, Via Mezzocannone 16, I-80134, Napoli, Italy

    G. Marino  & G. Sannia  & 

  2. Dipartimento di Scienze Biochimiche, Università di Roma “La Sapienza”, P.le Aldo Moro 5, I-00185, Roma, Italy

    F. Bossa

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© 1994 Birkhäuser Verlag Basel/Switzerland

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Cite this paper

Isupov, M. et al. (1994). X-ray study of tryptophanase at 2.1 Å resolution. In: Marino, G., Sannia, G., Bossa, F. (eds) Biochemistry of Vitamin B6 and PQQ. Advances in Life Sciences. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-7393-2_29

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  • DOI: https://doi.org/10.1007/978-3-0348-7393-2_29

  • Publisher Name: Birkhäuser Basel

  • Print ISBN: 978-3-0348-7395-6

  • Online ISBN: 978-3-0348-7393-2

  • eBook Packages: Springer Book Archive

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