1KH1

Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase

1KH1 の概要

• エントリーDOI: 10.2210/pdb1kh1/pdb
• 関連するPDBエントリー: 1KH2 1KH3
• 分子名称: Argininosuccinate Synthetase, SULFATE ION (3 entities in total)
• 機能のキーワード: ligase, riken structural genomics/proteomics initiative, rsgi, structural genomics
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 179888.22

構造登録者

Goto, M.,Nakajima, Y.,Hirotsu, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2001-11-29, 公開日: 2002-04-03, 最終更新日: 2024-03-13)

主引用文献

Goto, M.,Nakajima, Y.,Hirotsu, K.
Crystal structure of argininosuccinate synthetase from Thermus thermophilus HB8. Structural basis for the catalytic action.
J.Biol.Chem., 277:15890-15896, 2002

PubMed Abstract: Argininosuccinate synthetase catalyzes the ATP-dependent condensation of a citrulline with an aspartate to give argininosuccinate. The three-dimensional structures of the enzyme from Thermus thermophilus HB8 in its free form, complexed with intact ATP, and complexed with an ATP analogue (adenylyl imidodiphosphate) and substrate analogues (arginine and succinate) have been determined at 2.3-, 2.3-, and 1.95-A resolution, respectively. The structure is essentially the same as that of the Escherichia coli argininosuccinate synthetase. The small domain has the same fold as that of a new family of "N-type" ATP pyrophosphatases with the P-loop specific for the pyrophosphate of ATP. However, the enzyme shows the P-loop specific for the gamma-phosphate of ATP. The structure of the complex form is quite similar to that of the native one, indicating that no conformational change occurs upon the binding of ATP and the substrate analogues. ATP and the substrate analogues are bound to the active site with their reaction sites close to one another and located in a geometrical orientation favorable to the catalytic action. The reaction mechanism so far proposed seems to be consistent with the locations of ATP and the substrate analogues. The reaction may proceed without the large conformational change of the enzyme proposed for the catalytic process.

PubMed: 11844799
DOI: 10.1074/jbc.M112430200

実験手法

X-RAY DIFFRACTION (2.3 Å)