Aminoacyl tRNA synthetases, class II
| Aminoacyl-tRNA synthetase, class II (D, K and N) | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||
| Symbol | aa-tRNA-synt_II | ||||||||||
| Pfam | PF00152 | ||||||||||
| InterPro | IPR004364 | ||||||||||
| CDD | cd00768 | ||||||||||
| |||||||||||
Aminoacyl-tRNA synthetase, class II (D, K and N) (EC 6.1.1.) is a protein domain that catalyses the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. This protein differs widely in size and oligomeric state, and has a limited sequence homology.[1]
The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric.[2] Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices,[3] and are mostly dimeric or multimeric, containing at least three conserved regions.[4][5][6] However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan and valine belong to class I synthetases; these synthetases are further divided into three subclasses, a, b and c, according to sequence homology. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine belong to class-II synthetases.[7]
Human proteins containing this domain
References
- ^ Delarue M, Moras D, Poch O, Eriani G, Gangloff J (1990). "Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs". Nature. 347 (6289): 203–206. doi:10.1038/347203a0. PMID 2203971.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Moras D, Konno M, Shimada A, Nureki O, Tateno M, Yokoyama S, Sugiura I, Ugaji-Yoshikawa Y, Kuwabara S, Lorber B, Giege R (2000). "The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules". Structure. 8 (2): 197–208. doi:10.1016/S0969-2126(00)00095-2. PMID 10673435.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Perona JJ, Steitz TA, Rould MA (1993). "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase". Biochemistry. 32 (34): 8758–8771. doi:10.1021/bi00085a006. PMID 8364025.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Delarue M, Moras D (1993). "The aminoacyl-tRNA synthetase family: modules at work". BioEssays. 15 (10): 675–687. doi:10.1002/bies.950151007. PMID 8274143.
- ^ Schimmel P (1991). "Classes of aminoacyl-tRNA synthetases and the establishment of the genetic code". Trends Biochem. Sci. 16 (1): 1–3. doi:10.1016/0968-0004(91)90002-D. PMID 2053131.
- ^ Cusack S, Leberman R, Hartlein M (1991). "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases". Nucleic Acids Res. 19 (13): 3489–3498. doi:10.1093/nar/19.13.3489. PMC 328370. PMID 1852601.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Bairoch A (2004). "List of aminoacyl-tRNA synthetases": –.
{{cite journal}}: Cite journal requires|journal=(help)
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