| http://purl.uniprot.org/citations/10735864 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10735864 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10735864 | http://www.w3.org/2000/01/rdf-schema#comment | "In vivo recombination has been used to make a series of AroP-PheP chimeric proteins. Analysis of their respective substrate profiles and activities has identified a small region within span III of AroP which can confer on a predominantly PheP protein the ability to transport tryptophan. Site-directed mutagenesis of the AroP-PheP chimera, PheP, and AroP has established that a key residue involved in tryptophan transport is tyrosine at position 103 in AroP. Phenylalanine is the residue at the corresponding position in PheP. The use of PheP-specific antisera has shown that the inability of certain chimeras to transport any of the aromatic amino acids is not a result of instability or a failure to be inserted into the membrane. Site-directed mutagenesis has identified two significant AroP-specific residues, alanine 107 and valine 114, which are the direct cause of loss of transport activity in chimeras such as A152P. These residues replace a glycine and an alanine in PheP and flank a highly conserved glutamate at position 110. Some suggestions are made as to the possible functions of these residues in the tertiary structure of the proteins."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.182.8.2207-2217.2000"xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.182.8.2207-2217.2000"xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/author | "Pittard A.J."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/author | "Pittard A.J."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/author | "Dogovski C."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/author | "Dogovski C."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/author | "Brasier G."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/author | "Brasier G."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/author | "Cosgriff A.J."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/author | "Cosgriff A.J."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/author | "Pi J."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/author | "Pi J."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/author | "Sarsero J.P."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/author | "Sarsero J.P."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/pages | "2207-2217"xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/pages | "2207-2217"xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/title | "A study of AroP-PheP chimeric proteins and identification of a residue involved in tryptophan transport."xsd:string |
| http://purl.uniprot.org/citations/10735864 | http://purl.uniprot.org/core/title | "A study of AroP-PheP chimeric proteins and identification of a residue involved in tryptophan transport."xsd:string |