1999
DOI: 10.1016/s0014-5793(99)00860-1
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2.0 Å X‐ray structure of the ternary complex of 7,8‐dihydro‐6‐hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue

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 î 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 L LK KL LL LK KL L motif present in several other proteins including nucleoside diphosphate kinase. Comparative sequence examination of a … Show more

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Cited by 49 publications
(69 citation statements)
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“…1b) was found in the structure of the complex apparently due to the hydrolysis of the nucleotide. As previously predicted (1) and observed (3,5), the adenine base of ADP is positioned in the V-shaped cleft between ␤4 and ␤6 and the ribose and pyrophosphate extend along the valley and across ␤4 and ␤1 (Fig. 1a).…”
Section: Crystal Structure Of Hppk⅐mgadp At 15-å Resolutionsupporting
confidence: 87%
See 1 more Smart Citation
“…1b) was found in the structure of the complex apparently due to the hydrolysis of the nucleotide. As previously predicted (1) and observed (3,5), the adenine base of ADP is positioned in the V-shaped cleft between ␤4 and ␤6 and the ribose and pyrophosphate extend along the valley and across ␤4 and ␤1 (Fig. 1a).…”
Section: Crystal Structure Of Hppk⅐mgadp At 15-å Resolutionsupporting
confidence: 87%
“…The key elements responsible for pulling down the carboxyl group of Asp 95 appear to be the two bound Mg 2ϩ ions. One Mg 2ϩ is coordinated with the ␣-and ␤-phosphoryl groups of ATP, and the other with the ␤-and ␥-phosphoryl groups of ATP and the hydroxyl group of HP (3,5 Fig. 8b), and so is its coordination.…”
Section: Discussionmentioning
confidence: 99%
“…However, the 3′-OH group of GDP or GTP is by itself a rather unreactive species that requires activation via deprotonation, enforced by Glu139 and a magnesium ion. Similar activation of hydroxyl groups has been observed in hydroxymethylpterin pyrophosphokinases (HPPKs) (33). Taken together, these observations show that alarmone synthetases position their substrates in a geometry ideal for catalysis.…”
Section: Discussionsupporting
confidence: 74%
“…The structure of E. coli hydroxymethyldihydropterin diphosphokinase with a variety of ligands has been determined: these include the ternary complex with a substrate analog and a substrate, enzyme-Mg 2ϩ -␣,␤-methylene ATP-hydroxydihydropterin complex (PDB code 1q0n) (164). Additional reports on crystal or solution structures of hydroxymethyldihydropterin diphosphokinase of E. coli and Haemophilus influenzae have been published (165)(166)(167). Structural and mechanistic properties of this enzyme have been previously reviewed (168).…”
Section: Substitution Reactions At ␣- ␤- or ␥-Phosphatesmentioning
confidence: 99%