5HIW

Sorangium cellulosum So Ce56 cytochrome P450 260B1

5HIW の概要

• エントリーDOI: 10.2210/pdb5hiw/pdb
• 分子名称: Cytochrome P450 CYP260B1, PROTOPORPHYRIN IX CONTAINING FE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: p450, cytochrome, cyp, sorangium, 260b1, steroids, oxidoreductase
• 由来する生物種: Sorangium cellulosum (strain So ce56)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44211.78

構造登録者

Salamanca-Pinzon, S.G.,Carius, Y.,Khatri, Y.,Bernhardt, R.,Lancaster, C.R.D. (登録日: 2016-01-12, 公開日: 2016-08-03, 最終更新日: 2024-01-10)

主引用文献

Salamanca-Pinzon, S.G.,Khatri, Y.,Carius, Y.,Keller, L.,Muller, R.,Lancaster, C.R.,Bernhardt, R.
Structure-function analysis for the hydroxylation of Delta 4 C21-steroids by the myxobacterial CYP260B1.
Febs Lett., 590:1838-1851, 2016

PubMed Abstract: Myxobacterial CYP260B1 from Sorangium cellulosum was heterologously expressed in Escherichia coli and purified. The in vitro conversion of a small focused substrate library comprised of Δ4 C21-steroids and steroidal drugs using surrogate bovine redox partners shows that CYP260B1 is a novel steroid hydroxylase. CYP260B1 performs the regio- and stereoselective hydroxylation of the glucocorticoid cortodoxone (RSS) to produce 6β-OH-RSS. The substrate-free crystal structure of CYP260B1 (PDB 5HIW) was resolved. Docking of the tested ligands into the crystal structure suggested that the C17 hydroxy moiety and the presence of either a keto or a hydroxy group at C11 determine the selectivity of hydroxylation.

PubMed: 27177597
DOI: 10.1002/1873-3468.12217

実験手法

X-RAY DIFFRACTION (1.85 Å)