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Literature summary for 6.1.1.15 extracted from

  • Crepin, T.; Yaremchuk, A.; Tukalo, M.; Cusack, S.
    Structures of two bacterial prolyl-tRNA synthetases with and without a cis-editing domain (2006), Structure, 14, 1511-1525.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Rhodopseudomonas palustris
expression of the enzyme in Escherichia coli strain M15 Enterococcus faecalis

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged wild-type and selenomethionine-labeled enzymes, hanging drop vapour diffusion method, mixing of protein solution containing 5 mg/ml with an equal volume of the reservoir solution containing 0.1 M citric acid, pH 5.5, 15%-17% PEG 3000, cryoprotection by 20% ethylene glycol, for PrsRp-adenylate analog complex cocrystals, the enzyme is mixed first with 500 nM ProAMS or 100 nM CysAMS, and then with an equal volume of a solution containing 0.1 M citric acid, pH 5.5, 10%-11% PEG 3000, 15%-20% ethylene glycol, X-ray diffraction structure determination and analysis at 2.9 A resolution Rhodopseudomonas palustris

Inhibitors

Inhibitors Comment Organism Structure
5'-O-(N-[prolyl]-sulphamoyl) adenosine i.e. ProAMS, a nonhydrolyzable analogue of the prolyl-adenylate Enterococcus faecalis
5'-O-(N-[prolyl]-sulphamoyl) adenosine i.e. ProAMS, a nonhydrolyzable analogue of the prolyl-adenylate Rhodopseudomonas palustris

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Enterococcus faecalis
Mg2+
-
Rhodopseudomonas palustris

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-proline + tRNAPro Enterococcus faecalis
-
AMP + diphosphate + L-prolyl-tRNAPro
-
?
ATP + L-proline + tRNAPro Rhodopseudomonas palustris
-
AMP + diphosphate + L-prolyl-tRNAPro
-
?

Organism

Organism UniProt Comment Textmining
Enterococcus faecalis Q831W7
-
-
Rhodopseudomonas palustris Q6N5P6
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain M15 by ammonium sulfate fractionation and anion exchange chromatography Enterococcus faecalis
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Rhodopseudomonas palustris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-proline + tRNAPro
-
Enterococcus faecalis AMP + diphosphate + L-prolyl-tRNAPro
-
?
ATP + L-proline + tRNAPro
-
Rhodopseudomonas palustris AMP + diphosphate + L-prolyl-tRNAPro
-
?
ATP + L-proline + tRNAPro small-substrate recognition by the prokaryote-type ProRS, model for posttransfer editing conformation, overview Enterococcus faecalis AMP + diphosphate + L-prolyl-tRNAPro
-
?
ATP + L-proline + tRNAPro small-substrate recognition by the prokaryote-type ProRS, model for posttransfer editing conformation, overview Rhodopseudomonas palustris AMP + diphosphate + L-prolyl-tRNAPro
-
?
additional information comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview Enterococcus faecalis ?
-
?
additional information comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview Rhodopseudomonas palustris ?
-
?

Subunits

Subunits Comment Organism
More comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, cognate and noncognate adenylate analogue complexes, overview Rhodopseudomonas palustris
More comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview Enterococcus faecalis

Synonyms

Synonyms Comment Organism
Prolyl-tRNA synthetase
-
Enterococcus faecalis
Prolyl-tRNA synthetase
-
Rhodopseudomonas palustris
ProRS
-
Enterococcus faecalis
ProRS
-
Rhodopseudomonas palustris

Cofactor

Cofactor Comment Organism Structure
ATP binding structure and complex formation with cognate tRNA, overview Enterococcus faecalis
ATP binding structure and complex formation with cognate tRNA, overview Rhodopseudomonas palustris