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Literature summary for 6.1.1.11 extracted from

  • Belrhali, H.; Yaremchuk, A.; Tukalo, M.; Berthet-Colominas, C.; Rasmussen, B.; Bösecke, P.; Diat, O.; Cusack, S.
    The structural basis for seryl-adenylate and Ap4A synthesis by seryl-tRNA synthetase (1995), Structure, 3, 341-352.
    View publication on PubMed
Search for more literature for 6.1.1.11

Crystallization (Commentary)

Crystallization (Comment) Organism
structure at 2.3-2.6 A resolution, of enzyme complexes: 1. with ATP and Mn2+, 2. containing seryl-adenylate in the active site, 3. between the enzyme, Ap4A and Mn2+ Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ the enzyme complexes: 1. with ATP and Mn2+, 2. containing seryl-adenylate in the active site, 3. between the enzyme, Ap4A and Mn2+, exhibit a common Mn2+-site in which the cation is coordinated by two active-site residues in addition to the alpha-phosphate group from the bound ligands Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Thermus thermophilus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-serine + tRNASer
-
 Thermus thermophilus AMP + diphosphate + L-seryl-tRNASer
-
 ?
ATP + L-serine + tRNASer
-
 Escherichia coli AMP + diphosphate + L-seryl-tRNASer
-
 ?