1HKH

unligated gamma lactamase from an Aureobacterium species

1HKH の概要

• エントリーDOI: 10.2210/pdb1hkh/pdb
• 分子名称: GAMMA LACTAMASE, SULFATE ION (3 entities in total)
• 機能のキーワード: hydrolase, alpha/beta hydrolase, co-factor free haloperoxidase
• 由来する生物種: MICROBACTERIUM
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61948.65

構造登録者

Line, K.,Isupov, M.N.,Littlechild, J.A. (登録日: 2003-03-10, 公開日: 2004-03-30, 最終更新日: 2023-12-13)

主引用文献

Line, K.,Isupov, M.N.,Littlechild, J.A.
The crystal structure of a (-) gamma-lactamase from an Aureobacterium species reveals a tetrahedral intermediate in the active site.
J. Mol. Biol., 338:519-532, 2004

PubMed Abstract: The structure of the recombinant (-) gamma-lactamase from an Aureobacterium species has been solved at 1.73A resolution in the cubic space group F23 with unit cell parameters a=b=c=240.6A. The trimeric enzyme has an alpha/beta hydrolase fold and closely resembles the cofactor free haloperoxidases. The structure has been solved in complex with a covalently bound ligand originating from the host cell and also in the unligated form. The associated density in the former structure has been interpreted as the two-ring ligand (3aR,7aS)-3a,4,7,7a-tetrahydro-benzo [1,3] dioxol-2-one which forms a tetrahedral complex with OG of the catalytic Ser98. Soaks of these crystals with the industrial substrate gamma-lactam or its structural analogue, norcamphor, result in the displacement of the ligand from the enzyme active site, thereby allowing determination of the unligated structure. The presence of the ligand in the active site protects the enzyme from serine hydrolase inhibitors. Cyclic ethylene carbonate, the first ring of the ligand, was shown to be a substrate of the enzyme.

PubMed: 15081810
DOI: 10.1016/j.jmb.2004.03.001

実験手法

X-RAY DIFFRACTION (1.73 Å)