Structure-function relationship of type-IV prepilin peptidase of Pseudomonas aeruginosa - A review
Structure-function relationship of type-IV prepilin peptidase of Pseudomonas aeruginosa - A review
复制标题
DOI：
10.1016/s0378-1119(96)00830-x
复制
发表时间：
1997-06-11
期刊：
影响因子：
3.5
通讯作者：
Strom, MS
中科院分区：
文献类型：
--
作者：
Lory, S;Strom, MS
The bifunctional enzyme prepilin peptidase (PilD) from Pseudomonas aeruginosa is a key determinant in both type-IV pilus biogenesis and extracellular protein secretion, in its roles as a leader peptidase and MTase. It is responsible for endopeptidic cleavage of the unique leader peptides that characterize type-IV pilin precursors, as well as proteins with homologous leader sequences that are essential components of the general secretion pathway found in a variety of Gram-negative pathogens. Following removal of the leader peptides, the same enzyme is responsible for the second posttranslational modification that characterizes the type-IV pilins and their homologues, namely N-methylation of the newly exposed N-terminal amino acid residue. This review discusses some of the work begun in order to answer questions regarding the structure-function relationships of the active sites of this unique enzyme. (C) 1997 Elsevier Science B.V.
