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Ca 2+ ‐induced folding of a family I.3 lipase with repetitive Ca 2+ binding motifs at the C‐terminus
Author(s) -
Amada Kei,
Kwon Hyun-Ju,
Haruki Mitsuru,
Morikawa Masaaki,
Kanaya Shigenori
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03108-8
Subject(s) - chemistry , n terminus , lipase , folding (dsp implementation) , protein folding , c terminus , binding domain , biophysics , domain (mathematical analysis) , crystallography , biochemistry , stereochemistry , binding site , peptide sequence , enzyme , amino acid , biology , gene , mathematical analysis , mathematics , electrical engineering , engineering
In order to understand a role of the Ca 2+ ion on the structure and function of a Ca 2+ ‐dependent family I.3 lipase from Pseudomonas sp. MIS38, apo‐PML, holo‐PML, holo‐PML*, and the N‐terminal domain alone (N‐fragment) were prepared and biochemically characterized. Apo‐PML and holo‐PML represent refolded proteins in the absence and presence of the Ca 2+ ion, respectively. Holo‐PML* represents a holo‐PML dialyzed against 20 mM Tris–HCl (pH 7.5). The results suggest that the C‐terminal domain of PML is almost fully unfolded in the apo‐form and its folding is induced by Ca 2+ binding. The folding of this C‐terminal domain may be required to make a conformation of the N‐terminal catalytic domain functional.