Literature summary for 6.1.1.7 extracted from

Naganuma, M.; Sekine, S.; Fukunaga, R.; Yokoyama, S.
Unique protein architecture of alanyl-tRNA synthetase for aminoacylation, editing, and dimerization (2009), Proc. Natl. Acad. Sci. USA, 106, 8489-8494.

Crystallization (Commentary)

Crystallization (Comment)	Organism
AlaRS-DELTAC, comprising the aminoacylation, tRNA-recognition, and editing domains, and AlaRS-C, comprising the dimerization domain. The aminoacylation/tRNA-recognition domains contain an insertion incompatible with the class-specific tRNA-binding mode. The editing domain is fixed tightly via hydrophobic interactions to the aminoacylation/tRNA-recognition domains, on the side opposite from that in threonyl-tRNA synthetase. A groove formed between the aminoacylation/tRNA-recognition domains and the editing domain appears to be an alternative tRNA-binding site. The amino acid residues required for the G3:U70 base pair recognition are mapped in this groove. The dimerization domain consists of helical and globular subdomains. The helical subdomain mediates dimerization by forming a helixloophelix zipper. The globular subdomain, which is important for the aminoacylation and editing activities, has a positively-charged face suitable for tRNA binding	Archaeoglobus fulgidus

Crystallization (Comment)

Organism

AlaRS-DELTAC, comprising the aminoacylation, tRNA-recognition, and editing domains, and AlaRS-C, comprising the dimerization domain. The aminoacylation/tRNA-recognition domains contain an insertion incompatible with the class-specific tRNA-binding mode. The editing domain is fixed tightly via hydrophobic interactions to the aminoacylation/tRNA-recognition domains, on the side opposite from that in threonyl-tRNA synthetase. A groove formed between the aminoacylation/tRNA-recognition domains and the editing domain appears to be an alternative tRNA-binding site. The amino acid residues required for the G3:U70 base pair recognition are mapped in this groove. The dimerization domain consists of helical and globular subdomains. The helical subdomain mediates dimerization by forming a helixloophelix zipper. The globular subdomain, which is important for the aminoacylation and editing activities, has a positively-charged face suitable for tRNA binding

Archaeoglobus fulgidus

Protein Variants

Protein Variants	Comment	Organism
additional information	expression of truncated forms AlaRS-DELTAC, comprising the aminoacylation, tRNA-recognition, and editing domains, and AlaRS-C, comprising the dimerization domain	Archaeoglobus fulgidus

Organism

Organism	UniProt	Comment	Textmining
Archaeoglobus fulgidus	O28029	-	-

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Release 2023.1 (January 2023)