Literature summary for 6.1.1.18 extracted from

Fu, Y.; Kim, Y.; Jin, K.S.; Kim, H.S.; Kim, J.H.; Wang, D.; Park, M.; Jo, C.H.; Kwon, N.H.; Kim, D.; Kim, M.H.; Jeon, Y.H.; Hwang, K.Y.; Kim, S.; Cho, Y.
Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation (2014), Proc. Natl. Acad. Sci. USA, 111, 15084-15089 .

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Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of the enzyme in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified multisynthetase complex (MSC) subcomplex comprising ArgRS, glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)/p43, X-ray diffraction structure determination and analysis	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P47897	-	-

Subunits

Subunits	Comment	Organism
More	in the multisynthetase complex (MSC) subcomplex (RQA1 subcomplex) comprising arginyl-tRNA synthetase (ArgRS), glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 ((AIMP1)/p43), the N-terminal domain of ArgRS forms a long coiled-coil structure with the N-terminal helix of AIMP1 and anchors the C-terminal core of GlnRS, thereby playing a central role in assembly of the three components. The MSC complex is comprised of nine different aminoacyl-tRNA synthetases (ARSs) and three accessary proteins. This ternary RQA1 complex is further anchores to AIMP2/p38 through interaction with AIMP1. Importance of interactions between the N-terminal domains of ArgRS and AIMP1 for the assembly of the higher-order MSC protein complex. The N-terminal domain of human GlnRS interacts with ArgRS in the MSC, GlnRS is anchored to the complex by the interaction of its C-terminal core with the Hb helix of ArgRS, structure-function analysis, overview. ArgRS, GlnRS, and AIMP1 form a 1:1:1 ternary complex in the asymmetric unit, besides a trimeric, the RQA1 subcomplex also can form a hexameric structure	Homo sapiens

Synonyms

Synonyms	Comment	Organism
GlnRS	-	Homo sapiens
Glutaminyl-tRNA synthetase	-	Homo sapiens
QRS	-	Homo sapiens

General Information

General Information	Comment	Organism
additional information	in the multisynthetase complex (MSC) subcomplex (RQA1 subcomplex) comprising arginyl-tRNA synthetase (ArgRS), glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 ((AIMP1)/p43), the N-terminal domain of ArgRS forms a long coiled-coil structure with the N-terminal helix of AIMP1 and anchors the C-terminal core of GlnRS, thereby playing a central role in assembly of the three components. Mutation of AIMP1 destabilizes the N-terminal helix of ArgRS and abrogates its catalytic activity. The MSC complex is comprised of nine different aminoacyl-tRNA synthetases (ARSs) and three accessary proteins. Mutation of the N-terminal helix of ArgRS liberates GlnRS, which is known to control cell death. This ternary RQA1 complex is further anchores to AIMP2/p38 through interaction with AIMP1. Importance of interactions between the N-terminal domains of ArgRS and AIMP1 for the catalytic and noncatalytic activities of ArgRS and for the assembly of the higher-order MSC protein complex. The N-terminal domain of human GlnRS interacts with ArgRS in the MSC, GlnRS is anchored to the complex by the interaction of its C-terminal core with the Hb helix of ArgRS, structure-function analysis, overview. The RQA1 subcomplex also can form a hexameric structure	Homo sapiens

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Release 2023.1 (January 2023)