Linked Life Data

8650577

Source:http://linkedlifedata.com/resource/pubmed/id/8650577

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5269
pubmed:dateCreated
1996-7-25
pubmed:databankReference
pubmed:abstractText
Peridinin-chlorophyll-protein, a water-soluble light-harvesting complex that has a blue-green absorbing carotenoid as its main pigment, is present in most photosynthetic dinoflagellates. Its high-resolution (2.0 angstrom) x-ray structure reveals a noncrystallographic trimer in which each polypeptide contains an unusual jellyroll fold of the alpha-helical amino- and carboxyl-terminal domains. These domains constitute a scaffold with pseudo-twofold symmetry surrounding a hydrophobic cavity filled by two lipid, eight peridinin, and two chlorophyll a molecules. The structural basis for efficient excitonic energy transfer from peridinin to chlorophyll is found in the clustering of peridinins around the chlorophylls at van der Waals distances.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1788-91
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Structural basis of light harvesting by carotenoids: peridinin-chlorophyll-protein from Amphidinium carterae.
pubmed:affiliation
Fakultät für Biologie, Universität Konstanz, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't