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Literature summary 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)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.15 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

EC Number Inhibitors Comment Organism Structure
6.1.1.15 5'-O-(N-[prolyl]-sulphamoyl) adenosine i.e. ProAMS, a nonhydrolyzable analogue of the prolyl-adenylate Enterococcus faecalis
6.1.1.15 5'-O-(N-[prolyl]-sulphamoyl) adenosine i.e. ProAMS, a nonhydrolyzable analogue of the prolyl-adenylate Rhodopseudomonas palustris

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.15 Enterococcus faecalis Q831W7
-
-
6.1.1.15 Rhodopseudomonas palustris Q6N5P6
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.15 ATP + L-proline + tRNAPro
-
 Enterococcus faecalis AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
6.1.1.15 ATP + L-proline + tRNAPro
-
 Rhodopseudomonas palustris AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
6.1.1.15 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
-
 ?
6.1.1.15 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
-
 ?
6.1.1.15 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 ?
-
 ?
6.1.1.15 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

EC Number Subunits Comment Organism
6.1.1.15 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
6.1.1.15 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

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

Cofactor

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