PMID:10452528
| Citation |
Stammers, DK, Achari, A, Somers, DO, Bryant, PK, Rosemond, J, Scott, DL and Champness, JN (1999) 2.0 A X-ray structure of the ternary complex of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue. FEBS Lett. 456:49-53 |
|---|---|
| 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 A 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 betaalpha betabeta alphabeta 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. |
| Links | |
| Keywords |
Adenosine Triphosphate/chemistry; Adenosine Triphosphate/metabolism; Amino Acid Sequence; Binding Sites; Conserved Sequence; Crystallography, X-Ray; Dihydropteroate Synthase/chemistry; Dihydropteroate Synthase/metabolism; Diphosphotransferases/chemistry; Diphosphotransferases/metabolism; Escherichia coli/enzymology; Models, Molecular; Protein Conformation; Protein Folding; Pterins/chemistry; Pterins/metabolism |
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