Eur J Biochem. 2001 Apr;268(8):2246-52.

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

Ivens A, Mayans O, Szadkowski H, Wilmanns M, Kirschner K.

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Institut für Biochemie der Universität zu Köln, Germany; EMBL-Hamburg Outstation, Hamburg, Germany. andreas.ivens@uni-koeln.de

Abstract

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 A resolution and preliminary X-ray characterization was carried out. The crystals are suitable for structure determination.

PMID:: 11298741; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Anthranilate Phosphoribosyl-Transferase (Trpd)

PDB: 1O17

Source: Sulfolobus solfataricus

Method: X-Ray Diffraction

Resolution: 2.05 Å

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