1dy3
From Proteopedia
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TERNARY COMPLEX OF 7,8-DIHYDRO-6-HYDROXYMETHYLPTERINPYROPHOSPHOKINASE FROM ESCHERICHIA COLI WITH ATP AND A SUBSTRATE ANALOGUE.
Overview
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.
About this Structure
1DY3 is a [Single protein] structure of sequence from [Escherichia coli] with MG, ATP and 87Y as [ligands]. Active as [[1]], with EC number [2.7.6.3]. Full crystallographic information is available from [OCA].
Reference
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., Stammers DK, Achari A, Somers DO, Bryant PK, Rosemond J, Scott DL, Champness JN, FEBS Lett. 1999 Jul 30;456(1):49-53. PMID:10452528
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