Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
46
pubmed:dateCreated
2000-12-12
pubmed:abstractText
The membrane-bound complex of the Salmonella typhimurium histidine permease, an ABC transporter (or traffic ATPase), is composed of two membrane proteins, HisQ and HisM, and two identical copies of an ATP-hydrolyzing protein, HisP. We have developed a technique that monitors quantitatively the sulfhydryl modification levels within the intact complex, and we have used it to investigate whether the HisP subunits behave identically within the complex. We show here that they interact differently with various thiol-specific reagents, thus indicating that, despite being identical, they are arranged asymmetrically. The possible basis of this asymmetry is discussed. We have also analyzed the occurrence of conformational changes during various stages of the activity cycle using thiol-specific reagents, fluorescence measurements, and circular dichroism spectroscopy. Cys-51, located close to the ATP-binding pocket, reflects conformational changes upon binding of ATP but does not participate in changes involved in signaling and translocation. The latter are shown to cause secondary structure alterations, as indicated by changes in alpha-helices; tertiary structure alterations also occur, as shown by fluorescence studies.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/2-(4'-maleimidylanilino)naphthalene-..., http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Transport Systems, Basic, http://linkedlifedata.com/resource/pubmed/chemical/Anilino Naphthalenesulfonates, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Bicyclo Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Reagents, http://linkedlifedata.com/resource/pubmed/chemical/histidine permease, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/monobromobimane
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14183-95
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11087367-ATP-Binding Cassette Transporters, pubmed-meshheading:11087367-Adenosine Triphosphatases, pubmed-meshheading:11087367-Adenosine Triphosphate, pubmed-meshheading:11087367-Amino Acid Transport Systems, Basic, pubmed-meshheading:11087367-Anilino Naphthalenesulfonates, pubmed-meshheading:11087367-Bacterial Proteins, pubmed-meshheading:11087367-Bicyclo Compounds, pubmed-meshheading:11087367-Circular Dichroism, pubmed-meshheading:11087367-Macromolecular Substances, pubmed-meshheading:11087367-Membrane Proteins, pubmed-meshheading:11087367-Membrane Transport Proteins, pubmed-meshheading:11087367-Protein Conformation, pubmed-meshheading:11087367-Protein Structure, Secondary, pubmed-meshheading:11087367-Salmonella typhimurium, pubmed-meshheading:11087367-Spectrometry, Fluorescence, pubmed-meshheading:11087367-Sulfhydryl Compounds, pubmed-meshheading:11087367-Sulfhydryl Reagents, pubmed-meshheading:11087367-Ultraviolet Rays
pubmed:year
2000
pubmed:articleTitle
Nonequivalence of the nucleotide-binding subunits of an ABC transporter, the histidine permease, and conformational changes in the membrane complex.
pubmed:affiliation
Department of Molecular and Cell Biology, Division of Biochemistry and Molecular Biology, University of California, Berkeley, California 94720, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.