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Crystallization and preliminary X-ray crystallographic study of the editing domain of Thermus thermophilus isoleucyl-tRNA synthetase complexed with pre- and post-transfer editing-substrate analogues.
Acta Crystallogr D Biol Crystallogr. 2004 Oct; 60(Pt 10):1900-2.AC

Abstract

The CP1 domain (the editing domain) of isoleucyl-tRNA synthetase (IleRS) hydrolyzes misactivated Val-AMP in pre-transfer editing and mischarged Val-tRNA(Ile) in post-transfer editing. The CP1 domain of Thermus thermophilus IleRS was expressed in isolation, purified and cocrystallized with Val-AMS (a Val-AMP analogue) and with Val-2AA (a Val-tRNA(Ile) analogue). Two different expression constructs were used for each cocrystallization. The complex crystals with Val-AMS belong to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 102.00, c = 84.88 A. The asymmetric unit contains two molecules of the CP1 domain, with a corresponding crystal volume per protein weight of 2.7 A3 Da(-1) and a solvent content of 53.5%. The complex crystals with Val-2AA belong to the tetragonal space group P4(1)22, with unit-cell parameters a = b = 72.59, c = 83.68 A. The asymmetric unit contains one molecule of the CP1 domain, with a corresponding crystal volume per protein weight of 2.8 A3 Da(-1) and a solvent content of 55.8%. Data sets diffracting to 1.7 A resolution were collected from each single crystal at 100 K.

Authors+Show Affiliations

Fukunaga R
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.
Yokoyama S
No affiliation info available

MeSH

CrystallizationCrystallography, X-RayIsoleucine-tRNA LigaseProtein Structure, TertiaryRNA EditingTemperatureThermus thermophilus

Pub Type(s)

Journal Article

Language

eng

PubMed ID

15388946

Citation

Fukunaga, Ryuya, and Shigeyuki Yokoyama. "Crystallization and Preliminary X-ray Crystallographic Study of the Editing Domain of Thermus Thermophilus isoleucyl-tRNA Synthetase Complexed With Pre- and Post-transfer Editing-substrate Analogues." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 10, 2004, pp. 1900-2.
Fukunaga R, Yokoyama S. Crystallization and preliminary X-ray crystallographic study of the editing domain of Thermus thermophilus isoleucyl-tRNA synthetase complexed with pre- and post-transfer editing-substrate analogues. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 10):1900-2.
Fukunaga, R., & Yokoyama, S. (2004). Crystallization and preliminary X-ray crystallographic study of the editing domain of Thermus thermophilus isoleucyl-tRNA synthetase complexed with pre- and post-transfer editing-substrate analogues. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 10), 1900-2.
Fukunaga R, Yokoyama S. Crystallization and Preliminary X-ray Crystallographic Study of the Editing Domain of Thermus Thermophilus isoleucyl-tRNA Synthetase Complexed With Pre- and Post-transfer Editing-substrate Analogues. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 10):1900-2. PubMed PMID: 15388946.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray crystallographic study of the editing domain of Thermus thermophilus isoleucyl-tRNA synthetase complexed with pre- and post-transfer editing-substrate analogues. AU - Fukunaga,Ryuya, AU - Yokoyama,Shigeyuki, Y1 - 2004/09/23/ PY - 2004/07/14/received PY - 2004/08/06/accepted PY - 2004/9/25/pubmed PY - 2005/3/30/medline PY - 2004/9/25/entrez SP - 1900 EP - 2 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 10 N2 - The CP1 domain (the editing domain) of isoleucyl-tRNA synthetase (IleRS) hydrolyzes misactivated Val-AMP in pre-transfer editing and mischarged Val-tRNA(Ile) in post-transfer editing. The CP1 domain of Thermus thermophilus IleRS was expressed in isolation, purified and cocrystallized with Val-AMS (a Val-AMP analogue) and with Val-2AA (a Val-tRNA(Ile) analogue). Two different expression constructs were used for each cocrystallization. The complex crystals with Val-AMS belong to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 102.00, c = 84.88 A. The asymmetric unit contains two molecules of the CP1 domain, with a corresponding crystal volume per protein weight of 2.7 A3 Da(-1) and a solvent content of 53.5%. The complex crystals with Val-2AA belong to the tetragonal space group P4(1)22, with unit-cell parameters a = b = 72.59, c = 83.68 A. The asymmetric unit contains one molecule of the CP1 domain, with a corresponding crystal volume per protein weight of 2.8 A3 Da(-1) and a solvent content of 55.8%. Data sets diffracting to 1.7 A resolution were collected from each single crystal at 100 K. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15388946/Crystallization_and_preliminary_X_ray_crystallographic_study_of_the_editing_domain_of_Thermus_thermophilus_isoleucyl_tRNA_synthetase_complexed_with_pre__and_post_transfer_editing_substrate_analogues_ DB - PRIME DP - Unbound Medicine ER -