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
| Autor: | David L. Scott, D. O. Somers, J. Rosemond, David K. Stammers, P.K. Bryant, Aniruddha Achari, J.N. Champness |
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| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Conformational change Protein Folding Folate pathway Stereochemistry Protein Conformation Biophysics Drug target Peptide Anti-microbial Crystallography X-Ray Biochemistry 7 8-Dihydro-6-hydroxymethylpterinpyrophosphokinase chemistry.chemical_compound Residue (chemistry) Adenosine Triphosphate Structural Biology Genetics Escherichia coli Amino Acid Sequence Pterin Molecular Biology Ternary complex Conserved Sequence X-ray crystallography chemistry.chemical_classification Dihydropteroate Synthase Binding Sites biology Active site Cell Biology Nucleoside-diphosphate kinase Pterins Crystallography Enzyme chemistry biology.protein Diphosphotransferases |
| Zdroj: | FEBS letters. 456(1) |
| ISSN: | 0014-5793 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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