Literature summary for 6.3.5.6 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.

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Brugia malayi

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

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

Organism

Organism	UniProt	Comment	Textmining
Brugia malayi	A0A0J9Y417	-	-

Synonyms

Synonyms	Comment	Organism
AsnRS	-	Brugia malayi
Asparaginyl-tRNA synthetase	-	Brugia malayi

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)