Linked Life Data

16511297

Source:http://linkedlifedata.com/resource/pubmed/id/16511297

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 3
pubmed:dateCreated
2006-3-2
pubmed:abstractText
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.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
186-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Crystallization and preliminary crystallographic analysis of selenomethionine-labelled progesterone 5beta-reductase from Digitalis lanata Ehrh.
pubmed:affiliation
Lehrstuhl für Biotechnik, Institut für Biologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Henkestrasse 91, D-91052 Erlangen, Germany.
pubmed:publicationType
Journal Article