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

被引:41
作者
Meinnel, T
Lazennec, C
Dardel, F
Schmitter, JM
Blanquet, S
机构
[1] Laboratoire de Biochimie, U. Rech. Associee No. 1970 Ctr. N., Ecole Polytechnique
关键词
domain architecture; deletion; complementation; NMR; active site;
D O I
10.1016/0014-5793(96)00357-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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.
引用
收藏
页码:91 / 95
页数:5
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