Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus

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2001
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Ivens, Andreas
Szadkowski, Halina
Wilmanns, Matthias
Kirschner, Kasper
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European Journal of Biochemistry. 2001, 268(8), pp. 2246-2252. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1046/j.1432-1327.2001.02102.x
Zusammenfassung

Anthranilate phosphoribosyltransferase (TrpD; EC 2.4.2.18) from the hyperthermophilic archaeon Sulfolobus solfataricus (ssTrpD) was expressed in Escherichia coli, purified and crystallized. Analytical gel permeation chromatography revealed a homodimeric composition of the enzyme. The steady‐state kinetic characteristics suggest tight binding of the substrate anthranilic acid and efficient catalysis at the physiological growth temperature of S. solfataricus. Crystals of ssTrpD diffract to better than 2.6 Å resolution and preliminary X‐ray characterization was carried out. The crystals are suitable for structure determination.

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570 Biowissenschaften, Biologie
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anthranilate phosphoribosyltransferase; protein crystallization; Sulfolobus solfataricus; tryptophan biosynthesis
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ISO 690IVENS, Andreas, Olga MAYANS, Halina SZADKOWSKI, Matthias WILMANNS, Kasper KIRSCHNER, 2001. Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus. In: European Journal of Biochemistry. 2001, 268(8), pp. 2246-2252. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1046/j.1432-1327.2001.02102.x
BibTex
@article{Ivens2001-12-20Purif-42021,
  year={2001},
  doi={10.1046/j.1432-1327.2001.02102.x},
  title={Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus},
  number={8},
  volume={268},
  issn={0014-2956},
  journal={European Journal of Biochemistry},
  pages={2246--2252},
  author={Ivens, Andreas and Mayans, Olga and Szadkowski, Halina and Wilmanns, Matthias and Kirschner, Kasper}
}
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    <dcterms:abstract xml:lang="eng">Anthranilate phosphoribosyltransferase (TrpD; EC 2.4.2.18) from the hyperthermophilic archaeon Sulfolobus solfataricus (ssTrpD) was expressed in Escherichia coli, purified and crystallized. Analytical gel permeation chromatography revealed a homodimeric composition of the enzyme. The steady‐state kinetic characteristics suggest tight binding of the substrate anthranilic acid and efficient catalysis at the physiological growth temperature of S. solfataricus. Crystals of ssTrpD diffract to better than 2.6 Å resolution and preliminary X‐ray characterization was carried out. The crystals are suitable for structure determination.</dcterms:abstract>
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