2PLQ

Crystal structure of the amidase from geobacillus pallidus RAPc8

2PLQ の概要

• エントリーDOI: 10.2210/pdb2plq/pdb
• 分子名称: Aliphatic amidase (2 entities in total)
• 機能のキーワード: nitrilase fold, alpha-beta-beta-alpha, hydrolase
• 由来する生物種: Geobacillus pallidus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38640.83

構造登録者

Kimani, S.W.,Sewell, B.T.,Agarkar, V.B.,Sayed, M.F.,Cowan, D.A. (登録日: 2007-04-20, 公開日: 2007-05-01, 最終更新日: 2023-08-30)

主引用文献

Agarkar, V.B.,Kimani, S.W.,Cowan, D.A.,Sayed, M.F.,Sewell, B.T.
The quaternary structure of the amidase from Geobacillus pallidus RAPc8 is revealed by its crystal packing.
Acta Crystallogr.,Sect.F, 62:1174-1178, 2006

PubMed Abstract: The amidase from Geobacillus pallidus RAPc8, a moderate thermophile, is a member of the nitrilase enzyme superfamily. It converts amides to the corresponding acids and ammonia and has application as an industrial catalyst. RAPc8 amidase has been cloned and functionally expressed in Escherichia coli and has been purified by heat treatment and a number of chromatographic steps. The enzyme was crystallized using the hanging-drop vapour-diffusion method. Crystals produced in the presence of 1.2 M sodium citrate, 400 mM NaCl, 100 mM sodium acetate pH 5.6 were selected for X-ray diffraction studies. A data set having acceptable statistics to 1.96 A resolution was collected under cryoconditions using an in-house X-ray source. The space group was determined to be primitive cubic P4(2)32, with unit-cell parameter a = 130.49 (+/-0.05) A. The structure was solved by molecular replacement using the backbone of the hypothetical protein PH0642 from Pyrococcus horikoshii (PDB code 1j31) with all non-identical side chains substituted with alanine as a probe. There is one subunit per asymmetric unit. The subunits are packed as trimers of dimers with D3 point-group symmetry around the threefold axis in such a way that the dimer interface seen in the homologues is preserved.

PubMed: 17142891

実験手法

X-RAY DIFFRACTION (1.9 Å)