Angkawidjaja_2005_FEBS.Lett_579_4707

Reference

Title : Importance of a repetitive nine-residue sequence motif for intracellular stability and functional structure of a family I.3 lipase - Angkawidjaja_2005_FEBS.Lett_579_4707
Author(s) : Angkawidjaja C , Paul A , Koga Y , Takano K , Kanaya S
Ref : FEBS Letters , 579 :4707 , 2005
Abstract :

PML5 is a functional derivative of a family I.3 lipase from Pseudomonas sp. MIS38 and contains five repeats of a nine-residue sequence motif. Two aspartate residues within the second and third repetitive sequences of PML5 were replaced by Ala. The secretion level, intracellular accumulation level, and stability of the resultant mutant protein were greatly reduced as compared to those of PML5. In addition, this mutant protein was inactive and did not bind Ca2+ ion. We propose that the repetitive sequences of PML5 form a beta-roll structure in the cells and thereby contribute to the intracellular stability and secretion efficiency of the protein.

PubMedSearch : Angkawidjaja_2005_FEBS.Lett_579_4707
PubMedID: 16098975

Related information

Citations formats

Angkawidjaja C, Paul A, Koga Y, Takano K, Kanaya S (2005)
Importance of a repetitive nine-residue sequence motif for intracellular stability and functional structure of a family I.3 lipase
FEBS Letters 579 :4707

Angkawidjaja C, Paul A, Koga Y, Takano K, Kanaya S (2005)
FEBS Letters 579 :4707