Crystallization and preliminary crystallographic analysis of selenomethionine-labelled progesterone 5beta-reductase from Digitalis lanata Ehrh.
Progesterone 5beta-reductase (5beta-POR) catalyzes the reduction of progesterone to 5beta-pregnane-3,20-dione and is the first stereospecific enzyme in the putative biosynthetic pathway of Digitalis cardenolides. Selenomethionine-derivatized 5beta-POR from D. lanata was successfully overproduced and crystallized. The crystals belong to space group P4(3)2(1)2, with unit-cell parameters a = 71.73, c = 186.64 A. A MAD data set collected at 2.7 A resolution allowed the identification of six out of eight possible Se-atom positions. A first inspection of the MAD-phased electron-density map shows that 5beta-POR is a Rossmann-type reductase and the quality of the map is such that it is anticipated that a complete atomic model of 5beta-POR will readily be built.
Egerer-Sieber
Claudia
C
Lehrstuhl für Biotechnik, Institut für Biologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Henkestrasse 91, D-91052 Erlangen, Germany.
Herl
Vanessa
V
Müller-Uri
Frieder
F
Kreis
Wolfgang
W
Muller
Yves A
YA
D003460:Crystallization; D018360:Crystallography, X-Ray; D004070:Digitalis / Q000201:enzymology*; D010088:Oxidoreductases / Q000737:chemistry*; D012645:Selenomethionine / Q000737:chemistry*
D012645:Selenomethionine; D010088:Oxidoreductases; C090493:progesterone 5 beta-reductase