The C‐terminal domain of peptide deformylase is disordered and dispensable for activity

FEBS Letters

Schmitter, Jean-Marie¹  Lazennec, Christine¹  Blanquet, Sylvain¹  Dardel, Frederic¹  Meinnel, Thierry¹ 

[1] Laboratoire de Biochimie, Unité de Recherche Associée No. 1970 du Centre National de la Recherche Scientifique, Ecole Polytechnique, F-91128 Palaiseau cedex, France

关键词: Domain architecture;    Deletion;    Complementation;    NMR;    Active site;    D;    dimensional;    EDTA;    ethylene diamine tetraacetate;    Fo;    N-formyl;    NMR;    nuclear magnetic resonance;    NOESY;    nuclear Overhauser effect spectroscopy;    PAGE;    polyacrylamide gel electrophoresis;    PDF;    peptide deformylase;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(96)00357-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Upon trypsinolysis, the 18 C-terminal residues of Escherichia coli peptide deformylase were removed but the resulting form exhibited full activity. Moreover, a mutant fms gene encoding the first 145 out of the 168 residues of the enzyme was able to complement a fms(Ts) strain and exhibited full activity. Upon progressive truncation up to residue 139, both activity and stability decreased up to complete inactivation. Mutagenesis of residues of the 138–145 region highlights the importance of Leu-141 and Phe-142. N-Terminal deletions were also carried out. Beyond two residues off, the enzyme showed a dramatic instability. Finally, NMR and thermostability studies of the full-length enzyme and comparison to the 1–147 form strongly suggest that the dispensable residues are disordered in solution.

【 授权许可】

Unknown