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Literature summary extracted from

  • Crepin, T.; Peterson, F.; Haertlein, M.; Jensen, D.; Wang, C.; Cusack, S.; Kron, M.
    A hybrid structural model of the complete Brugia malayi cytoplasmic asparaginyl-tRNA synthetase (2011), J. Mol. Biol., 405, 1056-1069.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.5.6 expressed in Escherichia coli Brugia malayi

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.22 purified apo-AsnRS, AsnRS in complex with AsnAMS, and in complex with Mg2+, ATP, and l-Asp-beta-NOH, X-ray diffraction structure determination and analysis at 1.9-2.4 A resolution Brugia malayi
6.3.5.6 structures of the catalytically active N-terminally truncated enzyme (residues 112-548) is solved by X-ray crystallography. The N-terminal domain contains a structured region with a novel fold featuring a lysine-rich helix that is shown by NMR to interact with tRNA. This is connected by an unstructured tether to the remainder of the enzyme, which is highly similar to the known structure of bacterial AsnRS Brugia malayi

Protein Variants

EC Number Protein Variants Comment Organism
6.3.5.6 DELTA 1-112 structures of the catalytically active N-terminally truncated enzyme (residues 112-548) is solved by X-ray crystallography Brugia malayi

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.1.1.22 cytoplasm
-
 Brugia malayi 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.22 Mg2+ required Brugia malayi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.22 ATP + L-asparagine + tRNAAsn Brugia malayi
-
 AMP + diphosphate + L-asparaginyl-tRNAAsn
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.22 Brugia malayi
-
-
-
6.3.5.6 Brugia malayi A0A0J9Y417
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.22 ATP + L-asparagine + tRNAAsn
-
 Brugia malayi AMP + diphosphate + L-asparaginyl-tRNAAsn
-
 ?
6.1.1.22 ATP + L-asparagine + tRNAAsn AsnRS structure analysis shows binding of Mg2+-ATP in one active site and L-Asp-beta-NOH adenylate and Mg2+-diphosphate in the other active site. Active-site ordering and rearrangement during activation, overview. The AsnRSBm N-terminal extension binds tRNA, structure, overview Brugia malayi AMP + diphosphate + L-asparaginyl-tRNAAsn
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.22 More X-ray crystallography and NMR structure determination and analysis of full-length and catalytically active N-terminally truncated enzyme, DELTAAsnRSBm monomer, comprising residues 112-548, overview Brugia malayi

Synonyms

EC Number Synonyms Comment Organism
6.1.1.22 AsnRS
-
 Brugia malayi
6.1.1.22 Asparaginyl-tRNA synthetase
-
 Brugia malayi
6.1.1.22 class IIb asparaginyl-tRNA synthetase
-
 Brugia malayi
6.3.5.6 AsnRS
-
 Brugia malayi
6.3.5.6 Asparaginyl-tRNA synthetase
-
 Brugia malayi

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.22 ATP
-
 Brugia malayi