1HFK

Asparaginase from Erwinia chrysanthemi, hexagonal form with weak sulfate

1HFK の概要

• エントリーDOI: 10.2210/pdb1hfk/pdb
• 関連するPDBエントリー: 1HFJ 3PGA
• 分子名称: L-ASPARAGINE AMIDOHYDROLASE, SULFATE ION (3 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: ERWINIA CHRYSANTHEMI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70438.17

構造登録者

Lubkowski, J.,Palm, G.J.,Kozak, M.,Jaskolski, M.,Wlodawer, A. (登録日: 2000-12-05, 公開日: 2000-12-07, 最終更新日: 2023-12-13)

主引用文献

Jaskolski, M.,Kozak, M.,Lubkowski, J.,Palm, G.J.,Wlodawer, A.
Structures of Two Highly Homologous Bacterial L-Asparaginases: A Case of Enantiomorphic Space Groups
Acta Crystallogr.,Sect.D, 57:369-, 2001

PubMed Abstract: Quasi-enantiomorphic crystals of the Y25F mutant of Escherichia coli L-asparaginase and of the native Erwinia chrysanthemi L-asparaginase were obtained in the hexagonal space groups P6(5)22 and P6(1)22, respectively. The structures of these highly homologous enzymes were solved by molecular replacement and were refined with data extending to 2.2-2.5 A. These structures were compared with each other, as well as with other L-asparaginase structures previously observed with different crystal packing. It is concluded that the observed phenomenon, which is rare, was most likely to have arisen by chance.

PubMed: 11223513
DOI: 10.1107/S0907444900020175

実験手法

X-RAY DIFFRACTION (2.17 Å)