Cys-scanning mutagenesis: a novel approach to structure function relationships in polytopic membrane proteins
| dc.contributor.author | Frillingos, S. | en |
| dc.contributor.author | Sahin-Toth, M. | en |
| dc.contributor.author | Wu, J. | en |
| dc.contributor.author | Kaback, H. R. | en |
| dc.date.accessioned | 2015-11-24T19:25:40Z | |
| dc.date.available | 2015-11-24T19:25:40Z | |
| dc.identifier.issn | 0892-6638 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/22646 | |
| dc.rights | Default Licence | - |
| dc.subject | Alkylation | en |
| dc.subject | Amino Acid Sequence | en |
| dc.subject | Antibodies, Monoclonal/immunology | en |
| dc.subject | Bacterial Proteins/chemistry/*genetics | en |
| dc.subject | Binding Sites | en |
| dc.subject | Catalytic Domain | en |
| dc.subject | Cysteine | en |
| dc.subject | Escherichia coli/enzymology | en |
| dc.subject | *Escherichia coli Proteins | en |
| dc.subject | Glutamic Acid/metabolism | en |
| dc.subject | Ion Transport | en |
| dc.subject | Membrane Proteins/chemistry/*genetics | en |
| dc.subject | Membrane Transport Proteins/chemistry/*genetics | en |
| dc.subject | Models, Molecular | en |
| dc.subject | Molecular Sequence Data | en |
| dc.subject | *Monosaccharide Transport Proteins | en |
| dc.subject | *Mutagenesis, Site-Directed | en |
| dc.subject | Protein Conformation | en |
| dc.subject | Protein Structure, Secondary | en |
| dc.subject | Protons | en |
| dc.subject | Recombinant Fusion Proteins/chemistry/*genetics | en |
| dc.subject | Structure-Activity Relationship | en |
| dc.subject | *Symporters | en |
| dc.title | Cys-scanning mutagenesis: a novel approach to structure function relationships in polytopic membrane proteins | en |
| heal.abstract | The entire lactose permease of Escherichia coli, a polytopic membrane transport protein that catalyzes beta-galactoside/H+ symport, has been subjected to Cys-scanning mutagenesis in order to determine which residues play an obligatory role in the mechanism and to create a library of mutants with a single-Cys residue at each position of the molecule for structure/function studies. Analysis of the mutants has led to the following: 1) only six amino acid side chains play an irreplaceable role in the transport mechanism; 2) positions where the reactivity of the Cys replacement is increased upon ligand binding are identified; 3) positions where the reactivity of the Cys replacement is decreased by ligand binding are identified; 4) helix packing, helix tilt, and ligand-induced conformational changes are determined by using the library of mutants in conjunction with a battery of site-directed techniques; 5) the permease is a highly flexible molecule; and 6) a working model that explains coupling between beta-galactoside and H+ translocation. structure-function relationships in polytopic membrane proteins. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/9761772 | - |
| heal.identifier.secondary | http://www.fasebj.org/content/12/13/1281.full.pdf | - |
| heal.journalName | Faseb Journal | en |
| heal.journalType | peer-reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 1998 | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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