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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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Published in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2006-03, Vol.62 (3), p.186-188 |
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container_title | Acta crystallographica. Section F, Structural biology and crystallization communications |
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creator | Egerer-Sieber, Claudia Herl, Vanessa Müller-Uri, Frieder Kreis, Wolfgang Muller, Yves A. |
description | 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. |
doi_str_mv | 10.1107/S1744309106001916 |
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Section F, Structural biology and crystallization communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Egerer-Sieber, Claudia</au><au>Herl, Vanessa</au><au>Müller-Uri, Frieder</au><au>Kreis, Wolfgang</au><au>Muller, Yves A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary crystallographic analysis of selenomethionine-labelled progesterone 5β-reductase from Digitalis lanata Ehrh</atitle><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle><addtitle>Acta Cryst. F</addtitle><date>2006-03</date><risdate>2006</risdate><volume>62</volume><issue>3</issue><spage>186</spage><epage>188</epage><pages>186-188</pages><issn>1744-3091</issn><eissn>1744-3091</eissn><abstract>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. 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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 |
title | Crystallization and preliminary crystallographic analysis of selenomethionine-labelled progesterone 5β-reductase from Digitalis lanata Ehrh |
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