1T3M

Structure of the isoaspartyl peptidase with L-asparaginase activity from E. coli

1T3M の概要

• エントリーDOI: 10.2210/pdb1t3m/pdb
• 関連するPDBエントリー: 1jn9 1k2x
• 分子名称: Putative L-asparaginase, SODIUM ION, NITRATE ION, ... (5 entities in total)
• 機能のキーワード: type iii l-asparaginase, plant-type asparaginase, isoaspartyl peptidase, hydrolase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 67788.44

構造登録者

Prahl, A.,Pazgier, M.,Hejazi, M.,Lockau, W.,Lubkowski, J. (登録日: 2004-04-27, 公開日: 2004-07-13, 最終更新日: 2023-08-23)

主引用文献

Prahl, A.,Pazgier, M.,Hejazi, M.,Lockau, W.,Lubkowski, J.
Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli.
Acta Crystallogr.,Sect.D, 60:1173-1176, 2004

PubMed Abstract: The crystal structure of the Escherichia coli enzyme (EcAIII) with isoaspartyl dipeptidase and L-asparaginase activity has been solved and refined to a resolution of 1.65 angstroms, with crystallographic R-factor and Rfree values of 0.178 and 0.209, respectively. EcAIII belongs to the family of N-terminal hydrolases. The amino-acid sequence of EcAIII is homologous to those of putative asparaginases from plants. The structure of EcAIII is similar to the structures of glycosylasparaginases. The mature and catalytically active form of EcAIII is a heterotetramer consisting of two alpha-subunits and two beta-subunits. Both of the equivalent active sites present in the EcAIII tetramer is assisted by a metal-binding site. The metal cations, modelled here as Na+, have not previously been observed in glycosylasparaginases. This reported structure helps to explain the inability of EcAIII and other plant-type asparaginases to hydrolyze N4-(beta-N-acetylglucosaminyl)-L-asparagine, the substrate of glycosylasparaginases.

PubMed: 15159592
DOI: 10.1107/S0907444904003403

実験手法

X-RAY DIFFRACTION (1.65 Å)