3AJE

Crystal structure of S. tokodaii Sua5 complexed with L-threonine and AMPPNP

3AJE の概要

• エントリーDOI: 10.2210/pdb3aje/pdb
• 関連するPDBエントリー: 2EQA
• 分子名称: Putative uncharacterized protein ST1526, THREONINE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total)
• 機能のキーワード: trna modification t6a, structural genomics, riken structural genomics/proteomics initiative, rsgi, rna binding protein
• 由来する生物種: Sulfolobus tokodaii
• 細胞内の位置: Cytoplasm (Potential): Q970S6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39845.54

構造登録者

Kuratani, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2010-06-01, 公開日: 2011-04-13, 最終更新日: 2023-11-01)

主引用文献

Kuratani, M.,Kasai, T.,Akasaka, R.,Higashijima, K.,Terada, T.,Kigawa, T.,Shinkai, A.,Bessho, Y.,Yokoyama, S.
Crystal structure of Sulfolobus tokodaii Sua5 complexed with L-threonine and AMPPNP
Proteins, 79:2065-2075, 2011

PubMed Abstract: The hypermodified nucleoside N(6)-threonylcarbamoyladenosine resides at position 37 of tRNA molecules bearing U at position 36 and maintains translational fidelity in the three kingdoms of life. The N(6)-threonylcarbamoyl moiety is composed of L-threonine and bicarbonate, and its synthesis was genetically shown to require YrdC/Sua5. YrdC/Sua5 binds to tRNA and ATP. In this study, we analyzed the L-threonine-binding mode of Sua5 from the archaeon Sulfolobus tokodaii. Isothermal titration calorimetry measurements revealed that S. tokodaii Sua5 binds L-threonine more strongly than L-serine and glycine. The Kd values of Sua5 for L-threonine and L-serine are 9.3 μM and 2.6 mM, respectively. We determined the crystal structure of S. tokodaii Sua5, complexed with AMPPNP and L-threonine, at 1.8 Å resolution. The L-threonine is bound next to AMPPNP in the same pocket of the N-terminal domain. Thr118 and two water molecules form hydrogen bonds with AMPPNP in a unique manner for adenine-specific recognition. The carboxyl group and the side-chain hydroxyl and methyl groups of L-threonine are buried deep in the pocket, whereas the amino group faces AMPPNP. The L-threonine is located in a suitable position to react together with ATP for the synthesis of N(6)-threonylcarbamoyladenosine.

PubMed: 21538543
DOI: 10.1002/prot.23026

実験手法

X-RAY DIFFRACTION (1.8 Å)