cd00773

HisRS-like_core

CDD entry
Member databaseCDD
CDD typedomain
Short nameHisRS-like_core
Setclass_II_aaRS-like_core

Description

Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
[8, 3, 1, 4, 5, 2, 7, 6]

References

1.Genomics and the evolution of aminoacyl-tRNA synthesis. Ruan B, Ahel I, Ambrogelly A, Becker HD, Bunjun S, Feng L, Tumbula-Hansen D, Ibba M, Korencic D, Kobayashi H, Jacquin-Becker C, Mejlhede N, Min B, Raczniak G, Rinehart J, Stathopoulos C, Li T, Soll D. Acta Biochim. Pol. 48, 313-21, (2001). PMID: 11732603

2.The quaternary structure of the HisZ-HisG N-1-(5'-phosphoribosyl)-ATP transferase from Lactococcus lactis. Bovee ML, Champagne KS, Demeler B, Francklyn CS. Biochemistry 41, 11838-46, (2002). View articlePMID: 12269828

3.Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Wolf YI, Aravind L, Grishin NV, Koonin EV. Genome Res. 9, 689-710, (1999). View articlePMID: 10447505

4.A succession of substrate induced conformational changes ensures the amino acid specificity of Thermus thermophilus prolyl-tRNA synthetase: comparison with histidyl-tRNA synthetase. Yaremchuk A, Tukalo M, Grotli M, Cusack S. J. Mol. Biol. 309, 989-1002, (2001). View articlePMID: 11399074

5.Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation. Francklyn C, Perona JJ, Puetz J, Hou YM. RNA 8, 1363-72, (2002). View articlePMID: 12458790

6.Proteobacterial histidine-biosynthetic pathways are paraphyletic. Bond JP, Francklyn C. J. Mol. Evol. 50, 339-47, (2000). PMID: 10795825

7.An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine biosynthesis. Sissler M, Delorme C, Bond J, Ehrlich SD, Renault P, Francklyn C. Proc. Natl. Acad. Sci. U.S.A. 96, 8985-90, (1999). View articlePMID: 10430882

8.Eleven down and nine to go. Cusack S. Nat. Struct. Biol. 2, 824-31, (1995). View articlePMID: 7552701

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