Linked Life Data

1717452

Source:http://linkedlifedata.com/resource/pubmed/id/1717452

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
1991-11-8
pubmed:abstractText
Traffic ATPases constitute a superfamily of transporters that include prokaryotic permeases and medically important eukaryotic proteins, such as the multidrug resistance P-glycoprotein and the cystic fibrosis gene product. We present a structure-function analysis of a member of this superfamily, the prokaryotic histidine permease, using mutations generated both in vitro and in vivo, and assaying several biochemical functions. The analysis supports a previously predicted structural model and allows the assignment of specific functions to several predicted structural features. Mutations in the secondary structure features which form the nucleotide-binding pocket in general cause the loss of ATP binding activity. Mutations in the helical domain retain ATP binding activity. Several mutations have been identified which may affect the signaling mechanism between ATP hydrolysis and membrane translocation. We relate our findings to those emerging from the recent biochemical and genetic analyses of cystic fibrosis mutations.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18714-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1717452-ATP-Binding Cassette Transporters, pubmed-meshheading:1717452-Amino Acid Sequence, pubmed-meshheading:1717452-Amino Acid Transport Systems, Basic, pubmed-meshheading:1717452-Bacterial Proteins, pubmed-meshheading:1717452-Cells, Cultured, pubmed-meshheading:1717452-Cystic Fibrosis, pubmed-meshheading:1717452-Cystic Fibrosis Transmembrane Conductance Regulator, pubmed-meshheading:1717452-Genes, Suppressor, pubmed-meshheading:1717452-Humans, pubmed-meshheading:1717452-Membrane Proteins, pubmed-meshheading:1717452-Membrane Transport Proteins, pubmed-meshheading:1717452-Molecular Sequence Data, pubmed-meshheading:1717452-Mutagenesis, Site-Directed, pubmed-meshheading:1717452-Mutation, pubmed-meshheading:1717452-Sequence Alignment, pubmed-meshheading:1717452-Structure-Activity Relationship, pubmed-meshheading:1717452-Suppression, Genetic
pubmed:year
1991
pubmed:articleTitle
Structure-function analysis of the histidine permease and comparison with cystic fibrosis mutations.
pubmed:affiliation
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.