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2.0 Å X-ray structure of the ternary complex of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase fromEscherichia coliwith ATP and a substrate analogue

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
456
Issue
1
Identifiers
DOI: 10.1016/s0014-5793(99)00860-1
Keywords
  • Anti-Microbial
  • Folate Pathway
  • Drug Target
  • X-Ray Crystallography
  • 7
  • 8-Dihydro-6-Hydroxymethylpterinpyrophosphokinase
Disciplines
  • Biology

Abstract

Abstract The X-ray crystal structure of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase (PPPK) in a ternary complex with ATP and a pterin analogue has been solved to 2.0 Å resolution, giving, for the first time, detailed information of the PPPK/ATP intermolecular interactions and the accompanying conformational change. The first 100 residues of the 158 residue peptide contain a βαββαβ motif present in several other proteins including nucleoside diphosphate kinase. Comparative sequence examination of a wide range of prokaryotic and lower eukaryotic species confirms the conservation of the PPPK active site, indicating the value of this de novo folate biosynthesis pathway enzyme as a potential target for the development of novel broad-spectrum anti-infective agents.

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