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Literature summary for 2.7.6.3 extracted from

  • Blaszczyk, J.; Li, Y.; Shi, G.; Yan, H.; Ji, X.
    Dynamic roles of arginine residues 82 and 92 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: crystallographic studies (2003), Biochemistry, 42, 1573-1580.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor-diffusion method. At 0.89-A resolution, two distinct conformations are observed for each of the two residues in the crystal structure of the wild-type enzyme in complex with two 6-hydroxymethyl-7,8-dihydropterin variants, two Mg2+ ions, and an ATP analogue. 1. Complex of wild-type enzyme with 6-hydroxymethylpterin, 6-carboxypterin and alpha,beta-methyleneadenosine 5'-triphosphate, 2. complex of mutant enzyme R82A with 6-hydroxymethyl-7,8-dihydropterin and alpha,beta-methyleneadenosine 5'-triphosphate, 3. complex of mutant enzyme R92A with 6-hydroxymethyl-7,8-dihydropterin and alpha,beta-methyleneadenosine 5'-triphosphate, 4. matant apoenzyme of R82A, 5. mutant apoenzyme of R92A, 6. mutant enzyme R92A in complex with Mg2+ Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P26281
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-

Purification (Commentary)

Purification (Comment) Organism
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Escherichia coli

Synonyms

Synonyms Comment Organism
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
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Escherichia coli
HPPK
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Escherichia coli