Aminoacyl tRNA synthetases, class I

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	PDB: 1euq PDB: 1euy PDB: 1exd PDB: 1g59 PDB: 1gln PDB: 1gsg PDB: 1gtr PDB: 1gts PDB: 1irx PDB: 1j09

Glutamyl/glutaminyl-tRNA synthetase, class Ic
Glutamyl/glutaminyl-tRNA synthetase, class Ic
Identifiers
Symbol	Glu/Gln-tRNA-synth_Ic
Pfam	PF00749
InterPro	IPR000924
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	PDB: 1euq PDB: 1euy PDB: 1exd PDB: 1g59 PDB: 1gln PDB: 1gsg PDB: 1gtr PDB: 1gts PDB: 1irx PDB: 1j09

The aminoacyl-tRNA synthetases (EC 6.1.1.) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have 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]

Glutamyl-tRNA synthetase (EC 6.1.1.17) is a class Ic synthetase and shows several similarities with glutaminyl-tRNA synthetase concerning structure and catalytic properties. It is an alpha2 dimer. To date one crystal structure of a glutamyl-tRNA synthetase (Thermus thermophilus) has been solved. The molecule has the form of a bent cylinder and consists of four domains. The N-terminal half (domains 1 and 2) contains the 'Rossman fold' typical for class I synthetases and resembles the corresponding part of E. coli GlnRS, whereas the C-terminal half exhibits a GluRS-specific structure.^[8]

Human proteins containing this domain

EARS2; EPRS; PIG32; QARS;

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)
^ Soll D, Freist W, Gauss DH, Lapointe J (1997). "Glutamyl-tRNA sythetase". Biol. Chem. 378 (11): 1313–1329. doi:10.1515/bchm.1997.378.11.1299. PMID 9426192.{{cite journal}}: CS1 maint: multiple names: authors list (link)

This article incorporates text from the public domain Pfam and InterPro: IPR000924

[PUB00007191-1] 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)

[PUB00006477-2] 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)

[PUB00000386-3] 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)

[PUB00000723-4] 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.

[PUB00005365-5] 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.

[PUB00004391-6] 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)

[PUB00015156-7] Bairoch A (2004). "List of aminoacyl-tRNA synthetases": –. {{cite journal}}: Cite journal requires |journal= (help)

[PUB00006397-8] Soll D, Freist W, Gauss DH, Lapointe J (1997). "Glutamyl-tRNA sythetase". Biol. Chem. 378 (11): 1313–1329. doi:10.1515/bchm.1997.378.11.1299. PMID 9426192.{{cite journal}}: CS1 maint: multiple names: authors list (link)

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v t e Enzymes: CO CS and CN ligases (EC 6.1-6.3)
6.1: Carbon-Oxygen	Aminoacyl tRNA synthetase Alanine Arginine Asparagine Aspartate Cysteine D-alanine—poly(phosphoribitol) ligase Glutamate Glutamine Glycine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Proline Serine Threonine Tryptophan Tyrosine Valine
6.2: Carbon-Sulfur	Succinyl coenzyme A synthetase Acetyl—CoA synthetase Long-chain-fatty-acid—CoA ligase
6.3: Carbon-Nitrogen	Glutamine synthetase Ubiquitin ligase Cullin Von Hippel–Lindau tumor suppressor UBE3A Mdm2 Anaphase-promoting complex UBR1 Glutathione synthetase CTP synthetase Adenylosuccinate synthase Argininosuccinate synthase Holocarboxylase synthetase GMP synthase Asparagine synthetase Carbamoyl phosphate synthetase I II Glutamate–cysteine ligase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)