1PED

BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)

1PED の概要

• エントリーDOI: 10.2210/pdb1ped/pdb
• 分子名称: NADP-DEPENDENT ALCOHOL DEHYDROGENASE, ZINC ION (3 entities in total)
• 機能のキーワード: thermostable, oxidoreductase, zinc, nadp
• 由来する生物種: Clostridium beijerinckii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 151313.20

構造登録者

Korkhin, Y.,Frolow, F. (登録日: 1995-12-28, 公開日: 1997-07-07, 最終更新日: 2024-11-13)

主引用文献

Korkhin, Y.,Frolow, F.,Bogin, O.,Peretz, M.,Kalb, A.J.,Burstein, Y.
Crystalline alcohol dehydrogenases from the mesophilic bacterium Clostridium beijerinckii and the thermophilic bacterium Thermoanaerobium brockii: preparation, characterization and molecular symmetry.
Acta Crystallogr.,Sect.D, 52:882-886, 1996

PubMed Abstract: Two tetrameric NADP(+)-dependent bacterial secondary alcohol dehydrogenases have been crystallized in the apo- and the holo-enzyme forms. Crystals of the holo-enzyme from the mesophilic Clostridium beijerinckii (NCBAD) belong to space group P2(1)2(1)2(1) with unit-cell dimensions a = 90.5, b = 127.9, c = 151.4 A. Crystals of the apo-enzyme (CBAD) belong to the same space group with unit-cell dimensions a = 80.4, b = 102.3, c = 193.5 A. Crystals of the holo-enzyme from the thermophilic Thermoanaerobium brockii (NTBAD) belong to space group P6(1(5)) (a = b = 80.6, c = 400.7 A). Crystals of the apo-form of TBAD (point mutant GI98D) belong to space group P2(1) with cell dimensions a = 123.0, b = 84.8, c = 160.4 A beta = 99.5 degrees. Crystals of CBAD, NCBAD and NTBAD contain one tetramer per asymmetric unit. They diffract to 2.0 A resolution at liquid nitrogen temperature. Crystals of TBAD(GI98D) have two tetramers per asymmetric unit and diffract to 2.7 A at 276 K. Self-rotation analysis shows that both enzymes are tetramers of 222 symmetry.

PubMed: 15299659
DOI: 10.1107/S0907444996001461

実験手法

X-RAY DIFFRACTION (2.15 Å)