2CYC

Crystal structure of Tyrosyl-tRNA Synthetase complexed with L-tyrosine from Pyrococcus horikoshii

2CYC の概要

• エントリーDOI: 10.2210/pdb2cyc/pdb
• 分子名称: tyrosyl-tRNA synthetase, TYROSINE (3 entities in total)
• 機能のキーワード: tyrosine, tyrrs, aminoacylation, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, ligase
• 由来する生物種: Pyrococcus horikoshii
• 細胞内の位置: Cytoplasm (By similarity): O58739
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87047.07

構造登録者

Kuratani, M.,Sakai, H.,Takahashi, M.,Yanagisawa, T.,Kobayashi, T.,Sakamoto, K.,Terada, T.,Shirouzu, M.,Sekine, S.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2005-07-06, 公開日: 2005-11-22, 最終更新日: 2024-03-13)

主引用文献

Kuratani, M.,Sakai, H.,Takahashi, M.,Yanagisawa, T.,Kobayashi, T.,Murayama, K.,Chen, L.,Liu, Z.J.,Wang, B.C.,Kuroishi, C.,Kuramitsu, S.,Terada, T.,Bessho, Y.,Shirouzu, M.,Sekine, S.,Yokoyama, S.
Crystal Structures of Tyrosyl-tRNA Synthetases from Archaea
J.Mol.Biol., 355:395-408, 2006

PubMed Abstract: Tyrosyl-tRNA synthetase (TyrRS) catalyzes the tyrosylation of tRNA(Tyr) in a two-step reaction. TyrRS has the "HIGH" and "KMSKS" motifs, which play essential roles in the formation of the tyrosyl-adenylate from tyrosine and ATP. Here, we determined the crystal structures of Archaeoglobus fulgidus and Pyrococcus horikoshii TyrRSs in the l-tyrosine-bound form at 1.8A and 2.2A resolutions, respectively, and that of Aeropyrum pernix TyrRS in the substrate-free form at 2.2 A. The conformation of the KMSKS motif differs among the three TyrRSs. In the A.pernix TyrRS, the KMSKS loop conformation corresponds to the ATP-bound "closed" form. In contrast, the KMSKS loop of the P.horikoshii TyrRS forms a novel 3(10) helix, which appears to correspond to the "semi-closed" form. This conformation enlarges the entrance to the tyrosine-binding pocket, which facilitates the pyrophosphate ion release after the tyrosyl-adenylate formation, and probably is involved in the initial tRNA binding. The KMSSS loop of the A.fulgidus TyrRS is somewhat farther from the active site and is stabilized by hydrogen bonds. Based on the three structures, possible structural changes of the KMSKS motif during the tyrosine activation reaction are discussed. We suggest that the insertion sequence just before the KMSKS motif, which exists in some archaeal species, enhances the binding affinity of the TyrRS for its cognate tRNA. In addition, a non-proline cis peptide bond, which is involved in the tRNA binding, is conserved among the archaeal TyrRSs.

PubMed: 16325203
DOI: 10.1016/j.jmb.2005.10.073

実験手法

X-RAY DIFFRACTION (2.2 Å)