1DY3

Ternary complex of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue.

Summary for 1DY3

• Entry DOI: 10.2210/pdb1dy3/pdb
• Related: 1HKA
• Descriptor: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase, ADENOSINE-5'-TRIPHOSPHATE, 7,8-DIHYDRO-6-HYDROXYMETHYL-7-METHYL-7-[2-PHENYLETHYL]-PTERIN, ... (5 entities in total)
• Functional Keywords: pyrophosphorylase, de novo folate biosynthesis
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 18835.68

Authors

Stammers, D.K.,Achari, A.,Somers, D.O.,Bryant, P.K.,Rosemond, J.,Scott, D.L.,Champness, J.N. (deposition date: 2000-01-21, release date: 2000-08-18, Last modification date: 2024-05-08)

Primary citation

Stammers, D.K.,Achari, A.,Somers, D.O.,Bryant, P.K.,Rosemond, J.,Scott, D.L.,Champness, J.N.
2.0A 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-, 1999

PubMed 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.

PubMed: 10452528
DOI: 10.1016/S0014-5793(99)00860-1

Experimental method

X-RAY DIFFRACTION (2 Å)