Sequence‐imposed structural constraints in the TonB protein of E. coli

FEBS Letters

Levine, B.A.³  Dorman, C.J.¹  Higgins, C.F.¹  Evans, J.S.³  Trayer, I.P.² 

[1] Molecular Genetics Laboratory, Department of Biochemistry University of Dundee, Dundee DD1 4HN, Scotland;Department of Biochemistry, University of Birmingham, PO Box 363, Birmingham B1S 2TT, England;Inorganic Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QR, England

关键词: TonB protein Membrane protein Protein structure Praline1H-NMR;   

DOI  :  10.1016/0014-5793(86)81020-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown