1SET

CRYSTAL STRUCTURES AT 2.5 ANGSTROMS RESOLUTION OF SERYL-TRNA SYNTHETASE COMPLEXED WITH TWO DIFFERENT ANALOGUES OF SERYL-ADENYLATE

1SET の概要

• エントリーDOI: 10.2210/pdb1set/pdb
• 分子名称: SERYL-tRNA SYNTHETASE, 5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE (3 entities in total)
• 機能のキーワード: ligase, synthetase
• 由来する生物種: Thermus thermophilus
• 細胞内の位置: Cytoplasm (By similarity): P34945
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96624.46

構造登録者

Cusack, S.,Belrhali, H. (登録日: 1994-02-21, 公開日: 1994-07-31, 最終更新日: 2024-02-14)

主引用文献

Belrhali, H.,Yaremchuk, A.,Tukalo, M.,Larsen, K.,Berthet-Colominas, C.,Leberman, R.,Beijer, B.,Sproat, B.,Als-Nielsen, J.,Grubel, G.,Legrand, J.-F.,Lehmann, M.,Cusack, S.
Crystal structures at 2.5 angstrom resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate.
Science, 263:1432-1436, 1994

PubMed Abstract: Crystal structures of seryl-tRNA synthetase from Thermus thermophilus complexed with two different analogs of seryl adenylate have been determined at 2.5 A resolution. The first complex is between the enzyme and seryl-hydroxamate-AMP (adenosine monophosphate), produced enzymatically in the crystal from adenosine triphosphate (ATP) and serine hydroxamate, and the second is with a synthetic analog of seryl adenylate (5'-O-[N-(L-seryl)-sulfamoyl]adenosine), which is a strong inhibitor of the enzyme. Both molecules are bound in a similar fashion by a network of hydrogen bond interactions in a deep hydrophilic cleft formed by the antiparallel beta sheet and surrounding loops of the synthetase catalytic domain. Four regions in the primary sequence are involved in the interactions, including the motif 2 and 3 regions of class 2 synthetases. Apart from the specific recognition of the serine side chain, the interactions are likely to be similar in all class 2 synthetases.

PubMed: 8128224

実験手法

X-RAY DIFFRACTION (2.55 Å)