1O7J

Atomic resolution structure of Erwinia chrysanthemi L-asparaginase

1O7J の概要

• エントリーDOI: 10.2210/pdb1o7j/pdb
• 関連するPDBエントリー: 1HFJ 1HFK 1HFW 1HG0 1HG1 1JSL 1JSR
• 分子名称: L-ASPARAGINASE, SULFATE ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: l-asparaginase, atomic resolution, hydrolase
• 由来する生物種: ERWINIA CHRYSANTHEMI
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 142189.59

構造登録者

Lubkowski, J.,Dauter, M.,Aghaiypour, K.,Wlodawer, A.,Dauter, Z. (登録日: 2002-11-07, 公開日: 2002-12-04, 最終更新日: 2023-12-13)

主引用文献

Lubkowski, J.,Dauter, M.,Aghaiypour, K.,Wlodawer, A.,Dauter, Z.
Atomic Resolution Structure of Erwinia Chrysanthemi L-Asparaginase
Acta Crystallogr.,Sect.D, 59:84-, 2003

PubMed Abstract: An X-ray structure of L-asparaginase from Erwinia chrysanthemi (ErA) has been refined at 1 A resolution to an R factor of below 0.1, using data collected on a synchrotron source. With four molecules of the enzyme consisting of 327 amino acids each, this crystal contains one of the largest asymmetric units of a protein refined to date at atomic resolution. Previously, structures of ErA and of related enzymes from other bacterial sources have been refined at resolutions not exceeding 1.7 A; thus, the present structure represents a very significant improvement in the quality of the available models of these proteins and should provide a good basis for future studies of the conformational variability of proteins, identification of subtle conformational features and corroboration of the stereochemical libraries, amongst other things. L-Asparaginases, which are enzymes that catalyze the hydrolysis of L-asparagine to aspartic acid, have been used for over 30 y as therapeutic agents in the treatment of acute childhood lymphoblastic leukemia, although the details of the enzymatic reaction and substrate specificity have not yet been completely elucidated. This atomic resolution structure is a step in that direction.

PubMed: 12499544
DOI: 10.1107/S0907444902019443

実験手法

X-RAY DIFFRACTION (1 Å)