Linked Life Data

8241112

Source:http://linkedlifedata.com/resource/pubmed/id/8241112

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
46
pubmed:dateCreated
1993-12-23
pubmed:abstractText
The lactose permease of Escherichia coli is a paradigm for polytopic membrane transport proteins that transduce free energy stored in an electrochemical ion gradient into work in the form of a concentration gradient. Although the permease consists of 12 hydrophobic transmembrane domains in probable alpha-helical conformation that traverse the membrane in zigzag fashion connected by hydrophilic "loops", little information is available regarding the folded tertiary structure of the molecule. In this paper, we describe an approach to studying proximity relationships in lactose permease that is based upon site-directed pyrene labeling of combinations of paired Cys replacements in a mutant devoid of Cys residues. Since pyrene exhibits excimer fluorescence if two molecules are within about 3.5 A, the proximity between paired labeled residues can be determined. The results demonstrate that putative helices VIII and IX are close to helix X. Taken together with other findings indicating that helix VII is close to helices X and XI, the data lead to a model that describes the packing of helices VII-XI.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
32
pubmed:geneSymbol
lacY
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12273-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Use of site-directed fluorescence labeling to study proximity relationships in the lactose permease of Escherichia coli.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90024-1662.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't