Linked Life Data

3047112

Source:http://linkedlifedata.com/resource/pubmed/id/3047112

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
26
pubmed:dateCreated
1988-10-19
pubmed:abstractText
The isolation and deduced amino acid sequence of 70 melibiose carrier mutants with impaired methyl-beta-D-galactopyranoside (TMG) and cation recognition properties is described. The Km for TMG transport ranged from 1 to greater than 100 mM. Amino acid substitutions occurred at 23 unique sites within the protein. These sites were clustered into four distinct regions: Asp-15 through Ile-18 (cluster I), Tyr-116 through Pro-122 (cluster II), Val-342 through Ile-348 (cluster III), and Ala-364 through Gly-374. Only two sites fell outside of these clusters: Ile-61 and Ala-236. In the native conformation, some or all of these clusters may interact to form the substrate recognition site. Impairment of TMG recognition was accompanied by decreased Li+ inhibition of melibiose transport in all but one mutant. That changes in sugar recognition properties should so frequently accompany changes in cation recognition properties suggests an interaction between the two substrates. A model for such interaction is proposed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12909-15
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Mutations that simultaneously alter both sugar and cation specificity in the melibiose carrier of Escherichia coli.
pubmed:affiliation
Department of Cellular and Molecular Physiology, Harvard Medical School, Boston, Massachusetts 02115.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.