1dy3
From Proteopedia
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. 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 Page seeded by OCA on Fri May 2 14:25:18 2008
