2HLN

L-asparaginase from Erwinia carotovora in complex with glutamic acid

2HLN の概要

• エントリーDOI: 10.2210/pdb2hln/pdb
• 関連するPDBエントリー: 1ZCF 2GVN
• 分子名称: L-asparaginase, GLUTAMIC ACID, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: l-asparaginase, erwinia carotovora, hydrolase
• 由来する生物種: Pectobacterium atrosepticum
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 416953.70

構造登録者

Kravchenko, O.V.,Kislitsin, Y.A.,Popov, A.N.,Nikonov, S.V.,Kuranova, I.P. (登録日: 2006-07-08, 公開日: 2007-07-17, 最終更新日: 2023-08-30)

主引用文献

Kravchenko, O.V.,Kislitsin, Y.A.,Popov, A.N.,Nikonov, S.V.,Kuranova, I.P.
Three-dimensional structures of L-asparaginase from Erwinia carotovora complexed with aspartate and glutamate.
Acta Crystallogr.,Sect.D, 64:248-256, 2008

PubMed Abstract: The crystal structures of Erwinia carotovora L-asparaginase complexed with L-aspartate and L-glutamate were determined at 1.9 and 2.2 A, respectively, using the molecular-replacement method and were refined to R factors of about 21% in both cases. The positions of the ligands in the active site were located. A comparison of the new structures with the known structures of Escherichia coli L-asparaginase and Er. chrysanthemi L-asparaginase was performed. It was found that the arrangement of the ligands practically coincides in all three enzymes. The peculiarities of the quaternary structure of the enzyme, the possible role of water molecules in the enzyme action and the conformational changes during the catalyzed reaction are discussed.

PubMed: 18323619
DOI: 10.1107/S0907444907065766

実験手法

X-RAY DIFFRACTION (2.2 Å)