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Sequence‐imposed structural constraints in the TonB protein of E. coli
Author(s) -
Evans J.S.,
Levine B.A.,
Trayer I.P.,
Dorman C.J.,
Higgins C.F.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81020-1
Subject(s) - periplasmic space , bacterial outer membrane , biophysics , protein structure , peptide sequence , peptide , sequence (biology) , membrane protein , chemistry , crystallography , membrane , biochemistry , escherichia coli , biology , gene
The solution conformation of a 33‐residue peptide segment derived from the TonB protein which is implicated in bacterial membrane transport processes, has been investigated using high‐resolution proton magnetic resonance techniques. This proline‐rich peptide possesses sequence‐imposed sections of elongated secondary structure that must be retained in the native protein configuration. These structural constraints provide elements of stiffness that imply a purely structural role for TonB and are relevant to the subcellular location and biological role of the protein. On the basis of these data we suggest that this protein spans the periplasmic space linking the inner and outer membrane components of TonB‐dependent transport systems.