Crystallization and preliminary crystallographic analysis of selenomethionine-labelled progesterone 5β-reductase from Digitalis lanata Ehrh

Progesterone 5β‐reductase (5β‐POR) catalyzes the reduction of progesterone to 5β‐pregnane‐3,20‐dione and is the first stereospecific enzyme in the putative biosynthetic pathway of Digitalis cardenolides. Selenomethionine‐derivatized 5β‐POR from D. lanata was successfully overproduced and crystallize...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2006-03, Vol.62 (3), p.186-188
Main Authors: Egerer-Sieber, Claudia, Herl, Vanessa, Müller-Uri, Frieder, Kreis, Wolfgang, Muller, Yves A.
Format: Article
Language:English
Subjects:
ATOMS
CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
Crystallization Communications
CRYSTALS
DENSITY
Digitalis lanata
ELECTRON DENSITY
progesterone 5β-reductase
REDUCTION
RESOLUTION
SPACE GROUPS
SYNTHESIS
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Summary:Progesterone 5β‐reductase (5β‐POR) catalyzes the reduction of progesterone to 5β‐pregnane‐3,20‐dione and is the first stereospecific enzyme in the putative biosynthetic pathway of Digitalis cardenolides. Selenomethionine‐derivatized 5β‐POR from D. lanata was successfully overproduced and crystallized. The crystals belong to space group P43212, with unit‐cell parameters a = 71.73, c = 186.64 Å. A MAD data set collected at 2.7 Å 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 5β‐POR is a Rossmann‐type reductase and the quality of the map is such that it is anticipated that a complete atomic model of 5β‐POR will readily be built.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309106001916