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The leucine binding proteins of Escherichia coli as models for studying the relationships between protein structure and function
Author(s) -
Antonucci Tammy K.,
Landick Robert,
Oxender Dale L.
Publication year - 1985
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240290305
Subject(s) - periplasmic space , biochemistry , biology , leucine , escherichia coli , amino acid , valine , function (biology) , peptide sequence , binding protein , isoleucine , gene , microbiology and biotechnology
The genes encoding the leucine binding proteins in E coli have been cloned and their DNA sequences have been determined. One of the binding proteins (LIV‐BP) binds leucine, isoleucine, valine, threonine, and alanine, whereas the oilier (LS‐BP) binds only the D‐ and L‐isomers of leucine. These proteins bind their solutes as they enter the periplasm, then interact with three membrane components, livH, livG, and livM, to achieve the translocation of the solute across the bacterial cell membrane. Another feature of the binding proteins is that they must be secreted into the periplasmic space where they carry out their function. The amino acid sequence of the two binding proteins is 80% homologous, indicating that they arc the products of an ancestral gene duplication. Because of these characteristics of the leucine binding proteins, we are using them as models for studying the relationships between protein structure and function.