1N97

Crystal Structure of CYP175A1 from Thermus thermophillus strain HB27

1N97 の概要

• エントリーDOI: 10.2210/pdb1n97/pdb
• 分子名称: CYP175A1, S,R MESO-TARTARIC ACID, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• 機能のキーワード: p450, electron transport
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91294.94

構造登録者

Yano, J.K.,Blasco, F.,Li, H.,Schmid, R.D.,Henne, A.,Poulos, T.L. (登録日: 2002-11-22, 公開日: 2003-02-25, 最終更新日: 2023-08-16)

主引用文献

Yano, J.K.,Blasco, F.,Li, H.,Schmid, R.D.,Henne, A.,Poulos, T.L.
Preliminary Characterization and Crystal Structure of a Thermostable Cytochrome P450 from Thermus thermophilus
J.Biol.Chem., 278:608-616, 2003

PubMed Abstract: The second structure of a thermophile cytochrome P450, CYP175A1 from the thermophilic bacterium Thermus thermophilus HB27, has been solved to 1.8-A resolution. The overall P450 structure remains conserved despite the low sequence identity between the various P450s. The CYP175A1 structure lacks the large aromatic network found in the only other thermostable P450, CYP119, thought to contribute to thermal stability. The primary difference between CYP175A1 and its mesophile counterparts is the investment of charged residues into salt-link networks at the expense of single charge-charge interactions. Additional factors involved in the thermal stability increase are a decrease in the overall size, especially shortening of loops and connecting regions, and a decrease in the number of labile residues such as Asn, Gln, and Cys.

PubMed: 12401810
DOI: 10.1074/jbc.M206568200

実験手法

X-RAY DIFFRACTION (1.8 Å)