Maltose chemotaxis involves residues in the N-terminal and C-terminal domains on the same face of maltose-binding protein

Yinghua Zhang, Carol Conway, Margaret Rosato, Yousin Suh, Michael D. Manson

Research output: Contribution to journalArticle

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Abstract

The periplasmic maltose-binding protein (MBP) of Escherichia coli is the recognition component of the maltose chemoreceptor and of the active transport system for maltose. It interacts with the Tar chemotactic signal transducer and the integral cytoplasmic- membrane components (the MalF and MalG proteins) of the maltose transport system. Maltose binds in a cleft between the globular N-terminal and C-terminal domains of MBP, which are connected by a moveable hinge. The two domains undergo a large motion relative to one another as the protein moves from the open, unbound state to the closed, ligand-bound state. We generated, by doped-primer mutagenesis, amino acid substitutions that specifically disrupt the chemotactic function of MBP. These substitutions cluster in two well-defined regions that are nearly contiguous on the surface of MBP in its closed conformation. One region is in the N-terminal domain and one is in the C-terminal domain. The distance between the two regions is expected to change substantially as the protein goes from the open to the closed form. These results support a model in which ligand binding brings two recognition sites on MBP into the proper spatial relationship to interact with complementary sites on Tar. Mutations in MBP that appear to cause defects in interaction with MalF and MalG are distributed differently from mutations that primarily affect maltose taxis. We conclude that the regions of MBP that contact Tar and those that contact MalF and MaIG are adjacent on the face of the protein opposite the hinge connecting the two domains and that those regions are largely, although perhaps not entirely, distinct.

Original languageEnglish (US)
Pages (from-to)22813-22820
Number of pages8
JournalJournal of Biological Chemistry
Volume267
Issue number32
StatePublished - Nov 15 1992
Externally publishedYes

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Maltose-Binding Proteins
Maltose
Chemotaxis
Tars
Hinges
Proteins
Substitution reactions
Periplasmic Binding Proteins
Ligands
Mutagenesis
Mutation
Active Biological Transport
Protein Transport
Amino Acid Substitution
Transducers
Escherichia coli
Conformations
Cell Membrane
Membranes
Amino Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

Maltose chemotaxis involves residues in the N-terminal and C-terminal domains on the same face of maltose-binding protein. / Zhang, Yinghua; Conway, Carol; Rosato, Margaret; Suh, Yousin; Manson, Michael D.

In: Journal of Biological Chemistry, Vol. 267, No. 32, 15.11.1992, p. 22813-22820.

Research output: Contribution to journalArticle

Zhang, Yinghua ; Conway, Carol ; Rosato, Margaret ; Suh, Yousin ; Manson, Michael D. / Maltose chemotaxis involves residues in the N-terminal and C-terminal domains on the same face of maltose-binding protein. In: Journal of Biological Chemistry. 1992 ; Vol. 267, No. 32. pp. 22813-22820.
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