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Article

Genetic approach to the role of tryptophan residues in the activities and fluorescence of a bacterial periplasmic maltose-binding protein.

Journal of molecular biology - 5 Jul 1990

Martineau P, Szmelcman S, Spurlino J C, Quiocho F A, Hofnung M

Abstract excerpt

The periplasmic maltose-binding protein (MBP or MalE protein) of Escherichia coli is an essential element in the transport of maltose and maltodextrins and in the chemotaxis towards these sugars. On the basis of previous results suggesting their possible role in the activity and fluorescence of MBP, we have changed independently to alanine each of the eight tryptophan residues as well as asparagine 294, which is...

Topics

ATP-Binding Cassette Transporters
Alanine
Bacterial Proteins
Base Sequence
Biological Transport
Carbohydrate Sequence
Carrier Proteins
Chemotaxis
Escherichia coli
Escherichia coli Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Maltose

Maltose-Binding Proteins

Membrane Proteins

Models, Molecular

Molecular Sequence Data

Monosaccharide Transport Proteins

Mutation

Periplasmic Binding Proteins

Source

Identifiers

PMID: 2196376
DOI: 10.1016/0022-2836(90)90165-I

Genes

MBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2196376-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Genetic approach to the role of tryptophan residues in the activities and fluorescence of a bacterial periplasmic maltose-binding protein.PMID 2196376Read ↗

Progress in the identification of interaction sites on the periplasmic maltose binding protein from E coli.Semantic proximity Read ↗

The role of tryptophan residues in an integral membrane protein: diacylglycerol kinase.Semantic proximity Read ↗

Analysis of tryptophan residues in the staphylococcal multidrug transporter QacA reveals long-distance functional associations of residues on opposite sides of the membrane.Semantic proximity Read ↗

Unliganded maltose-binding protein triggers lactose transport in an Escherichia coli mutant with an alteration in the maltose transport system.Semantic proximity Read ↗

Effect of amino acid alterations in the tryptophan-binding site of the trp repressor.Semantic proximity Read ↗

Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor.Semantic proximity Read ↗

Maltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis.Semantic proximity Read ↗

Two modes of ligand binding in maltose-binding protein of Escherichia coli. Correlation with the structure of ligands and the structure of binding protein.Semantic proximity Read ↗

Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex.Semantic proximity Read ↗

Effects of mutations in the Pseudomonas putida miaA gene: regulation of the trpE and trpGDC operons in P. putida by attenuation.Semantic proximity Read ↗

Fluorescence properties of a tryptophan residue in an aromatic core of the protein subunit of ribonuclease P from Escherichia coli.Semantic proximity Read ↗

Crystallization of genetically engineered active maltose-binding proteins, including an immunogenic viral epitope insertion.Semantic proximity Read ↗

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