Loading…

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...

Full description

Saved in:
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:
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c4167-498de25e0d11db60a45dbaa5ae735decc0d80b0abb949917f9964c8bd59aa90e3
cites
container_end_page 188
container_issue 3
container_start_page 186
container_title Acta crystallographica. Section F, Structural biology and crystallization communications
container_volume 62
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
format article
fullrecord <record><control><sourceid>istex_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2197193</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>ark_67375_WNG_87ZZSXX1_H</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4167-498de25e0d11db60a45dbaa5ae735decc0d80b0abb949917f9964c8bd59aa90e3</originalsourceid><addsrcrecordid>eNqFkctu1TAQhiMEohd4AHaRWAfsOInjDVJ16AWpXKSCKN1YE3tyYvCxj2wXengGnoYH4ZlwlKoCsWBla-b_vpE9RfGEkmeUEv78gvKmYURQ0hFCBe3uFftzqZpr9_-47xUHMX4mhDHR9Q-LPdq1lNaC7xc_VmEXE1hrvkMy3pXgdLkNaM3GOAi7Ut32_TrAdjIqB8DuoomlH8uIFp3fYJoyahxWFga0FmeFX2NMGLzDsv31swqor1WCiOUY_KZ8adYma7PGZmGC8ngK06PiwQg24uPb87D4cHL8fnVWnb89fbU6Oq9UQzteNaLXWLdINKV66Ag0rR4AWkDOWo1KEd2TgcAwiEYIykchukb1g24FgCDIDosXi3d7PWxQK3QpgJXbYDb5ydKDkX93nJnk2n-VNRWcCpYFTxeBj8nIqExCNSnvHKok65q1HSNzii4pFXyMAce7CZTIeYHynwVmRizMN2Nx939AHn06qV-_awnhma0W1uSPv7ljIXyRHWe8lR_fnMqeX11dXF5SecZ-A9tEslA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Crystallization and preliminary crystallographic analysis of selenomethionine-labelled progesterone 5β-reductase from Digitalis lanata Ehrh</title><source>Open Access: PubMed Central</source><source>Wiley-Blackwell Read &amp; Publish Collection</source><creator>Egerer-Sieber, Claudia ; Herl, Vanessa ; Müller-Uri, Frieder ; Kreis, Wolfgang ; Muller, Yves A.</creator><creatorcontrib>Egerer-Sieber, Claudia ; Herl, Vanessa ; Müller-Uri, Frieder ; Kreis, Wolfgang ; Muller, Yves A.</creatorcontrib><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.</description><identifier>ISSN: 1744-3091</identifier><identifier>EISSN: 1744-3091</identifier><identifier>DOI: 10.1107/S1744309106001916</identifier><identifier>PMID: 16511297</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers</publisher><subject>ATOMS ; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY ; CRYSTALLIZATION ; Crystallization Communications ; CRYSTALS ; DENSITY ; Digitalis lanata ; ELECTRON DENSITY ; progesterone 5β-reductase ; REDUCTION ; RESOLUTION ; SPACE GROUPS ; SYNTHESIS</subject><ispartof>Acta crystallographica. Section F, Structural biology and crystallization communications, 2006-03, Vol.62 (3), p.186-188</ispartof><rights>International Union of Crystallography 2006 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4167-498de25e0d11db60a45dbaa5ae735decc0d80b0abb949917f9964c8bd59aa90e3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2197193/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2197193/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.osti.gov/biblio/22356303$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Egerer-Sieber, Claudia</creatorcontrib><creatorcontrib>Herl, Vanessa</creatorcontrib><creatorcontrib>Müller-Uri, Frieder</creatorcontrib><creatorcontrib>Kreis, Wolfgang</creatorcontrib><creatorcontrib>Muller, Yves A.</creatorcontrib><title>Crystallization and preliminary crystallographic analysis of selenomethionine-labelled progesterone 5β-reductase from Digitalis lanata Ehrh</title><title>Acta crystallographica. Section F, Structural biology and crystallization communications</title><addtitle>Acta Cryst. F</addtitle><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.</description><subject>ATOMS</subject><subject>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</subject><subject>CRYSTALLIZATION</subject><subject>Crystallization Communications</subject><subject>CRYSTALS</subject><subject>DENSITY</subject><subject>Digitalis lanata</subject><subject>ELECTRON DENSITY</subject><subject>progesterone 5β-reductase</subject><subject>REDUCTION</subject><subject>RESOLUTION</subject><subject>SPACE GROUPS</subject><subject>SYNTHESIS</subject><issn>1744-3091</issn><issn>1744-3091</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNqFkctu1TAQhiMEohd4AHaRWAfsOInjDVJ16AWpXKSCKN1YE3tyYvCxj2wXengGnoYH4ZlwlKoCsWBla-b_vpE9RfGEkmeUEv78gvKmYURQ0hFCBe3uFftzqZpr9_-47xUHMX4mhDHR9Q-LPdq1lNaC7xc_VmEXE1hrvkMy3pXgdLkNaM3GOAi7Ut32_TrAdjIqB8DuoomlH8uIFp3fYJoyahxWFga0FmeFX2NMGLzDsv31swqor1WCiOUY_KZ8adYma7PGZmGC8ngK06PiwQg24uPb87D4cHL8fnVWnb89fbU6Oq9UQzteNaLXWLdINKV66Ag0rR4AWkDOWo1KEd2TgcAwiEYIykchukb1g24FgCDIDosXi3d7PWxQK3QpgJXbYDb5ydKDkX93nJnk2n-VNRWcCpYFTxeBj8nIqExCNSnvHKok65q1HSNzii4pFXyMAce7CZTIeYHynwVmRizMN2Nx939AHn06qV-_awnhma0W1uSPv7ljIXyRHWe8lR_fnMqeX11dXF5SecZ-A9tEslA</recordid><startdate>200603</startdate><enddate>200603</enddate><creator>Egerer-Sieber, Claudia</creator><creator>Herl, Vanessa</creator><creator>Müller-Uri, Frieder</creator><creator>Kreis, Wolfgang</creator><creator>Muller, Yves A.</creator><general>Munksgaard International Publishers</general><general>International Union of Crystallography</general><scope>BSCLL</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>200603</creationdate><title>Crystallization and preliminary crystallographic analysis of selenomethionine-labelled progesterone 5β-reductase from Digitalis lanata Ehrh</title><author>Egerer-Sieber, Claudia ; Herl, Vanessa ; Müller-Uri, Frieder ; Kreis, Wolfgang ; Muller, Yves A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4167-498de25e0d11db60a45dbaa5ae735decc0d80b0abb949917f9964c8bd59aa90e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>ATOMS</topic><topic>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</topic><topic>CRYSTALLIZATION</topic><topic>Crystallization Communications</topic><topic>CRYSTALS</topic><topic>DENSITY</topic><topic>Digitalis lanata</topic><topic>ELECTRON DENSITY</topic><topic>progesterone 5β-reductase</topic><topic>REDUCTION</topic><topic>RESOLUTION</topic><topic>SPACE GROUPS</topic><topic>SYNTHESIS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Egerer-Sieber, Claudia</creatorcontrib><creatorcontrib>Herl, Vanessa</creatorcontrib><creatorcontrib>Müller-Uri, Frieder</creatorcontrib><creatorcontrib>Kreis, Wolfgang</creatorcontrib><creatorcontrib>Muller, Yves A.</creatorcontrib><collection>Istex</collection><collection>CrossRef</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. 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. 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.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Munksgaard International Publishers</pub><pmid>16511297</pmid><doi>10.1107/S1744309106001916</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1744-3091
ispartof Acta crystallographica. Section F, Structural biology and crystallization communications, 2006-03, Vol.62 (3), p.186-188
issn 1744-3091
1744-3091
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2197193
source Open Access: PubMed Central; Wiley-Blackwell Read & Publish Collection
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
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-01T10%3A51%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-istex_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystallization%20and%20preliminary%20crystallographic%20analysis%20of%20selenomethionine-labelled%20progesterone%205%CE%B2-reductase%20from%20Digitalis%20lanata%20Ehrh&rft.jtitle=Acta%20crystallographica.%20Section%20F,%20Structural%20biology%20and%20crystallization%20communications&rft.au=Egerer-Sieber,%20Claudia&rft.date=2006-03&rft.volume=62&rft.issue=3&rft.spage=186&rft.epage=188&rft.pages=186-188&rft.issn=1744-3091&rft.eissn=1744-3091&rft_id=info:doi/10.1107/S1744309106001916&rft_dat=%3Cistex_pubme%3Eark_67375_WNG_87ZZSXX1_H%3C/istex_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c4167-498de25e0d11db60a45dbaa5ae735decc0d80b0abb949917f9964c8bd59aa90e3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/16511297&rfr_iscdi=true