Pathways & interactions
Literature: Aminoacyl-tRNA synthetase, class Ic (IPR002305)
References used in this entry
The following publications were referred to in the abstract:
The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules.
Sugiura I, Nureki O, Ugaji-Yoshikawa Y, Kuwabara S, Shimada A, Tateno M, Lorber B, Giege R, Moras D, Yokoyama S, Konno M.
Structure 8 197-208 2000
PMID: 10673435 Related citations
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
PMID: 10447505 Related citations
Aminoacyl-tRNA synthetases: potential markers of genetic code development.
Ribas de Pouplana L, Schimmel P.
Trends Biochem. Sci. 26 591-6 2001
PMID: 11590011 Related citations
Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.
Perona JJ, Rould MA, Steitz TA.
Biochemistry 32 8758-71 1993
PMID: 8364025 Related citations
The aminoacyl-tRNA synthetase family: modules at work.
Delarue M, Moras D.
Bioessays 15 675-87 1993
PMID: 8274143 Related citations
Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.
Cusack S, Hartlein M, Leberman R.
Nucleic Acids Res. 19 3489-98 1991
PMID: 1852601 Related citations
Classes of aminoacyl-tRNA synthetases and the establishment of the genetic code.
Trends Biochem. Sci. 16 1-3 1991
PMID: 2053131 Related citations
Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs.
Eriani G, Delarue M, Poch O, Gangloff J, Moras D.
Nature 347 203-6 1990
PMID: 2203971 Related citations
Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process.
Woese CR, Olsen GJ, Ibba M, Soll D.
Microbiol. Mol. Biol. Rev. 64 202-36 2000
PMID: 10704480 Related citations
Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation.
Francklyn C, Perona JJ, Puetz J, Hou YM.
RNA 8 1363-72 2002
PMID: 12458790 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
Catalytic mechanism of the tryptophan activation reaction revealed by crystal structures of human tryptophanyl-tRNA synthetase in different enzymatic states.
Shen N, Zhou M, Yang B, Yu Y, Dong X, Ding J.
Nucleic Acids Res. 36 1288-99 2008
PMID: 18180246 Related citations
Independent saturation of three TrpRS subsites generates a partially assembled state similar to those observed in molecular simulations.
Laowanapiban P, Kapustina M, Vonrhein C, Delarue M, Koehl P, Carter CW Jr.
Proc. Natl. Acad. Sci. U.S.A. 106 1790-5 2009
PMID: 19174517 Related citations
Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase.
Doublie S, Bricogne G, Gilmore C, Carter CW Jr.
Structure 3 17-31 1995
PMID: 7743129 Related citations
Functional and crystal structure analysis of active site adaptations of a potent anti-angiogenic human tRNA synthetase.
Yang XL, Guo M, Kapoor M, Ewalt KL, Otero FJ, Skene RJ, McRee DE, Schimmel P.
Structure 15 793-805 2007
PMID: 17637340 Related citations
Blocking S-adenosylmethionine synthesis in yeast allows selenomethionine incorporation and multiwavelength anomalous dispersion phasing.
Malkowski MG, Quartley E, Friedman AE, Babulski J, Kon Y, Wolfley J, Said M, Luft JR, Phizicky EM, DeTitta GT, Grayhack EJ.
Proc. Natl. Acad. Sci. U.S.A. 104 6678-83 2007
PMID: 17426150 Related citations
Crystal structure of tryptophanyl-tRNA synthetase complexed with adenosine-5' tetraphosphate: evidence for distributed use of catalytic binding energy in amino acid activation by class I aminoacyl-tRNA synthetases.
Retailleau P, Weinreb V, Hu M, Carter CW Jr.
J. Mol. Biol. 369 108-28 2007
PMID: 17428498 Related citations