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Crystal structure of a family I.3 lipase from Pseudomonas sp. MIS38 in a closed conformation
Author(s) -
Angkawidjaja Clement,
You Dong-ju,
Matsumura Hiroyoshi,
Kuwahara Katsumasa,
Koga Yuichi,
Takano Kazufumi,
Kanaya Shigenori
Publication year - 2007
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/j.febslet.2007.09.048
Subject(s) - lipase , crystal structure , chemistry , crystallography , stereochemistry , serratia marcescens , pseudomonas , hydrolase , enzyme , biology , biochemistry , bacteria , escherichia coli , gene , genetics
The crystal structure of a family I.3 lipase from Pseudomonas sp. MIS38 in a closed conformation was determined at 1.5 Å resolution. This structure highly resembles that of Serratia marcescens LipA in an open conformation, except for the structures of two lids. Lid1 is anchored by a Ca 2+ ion (Ca1) in an open conformation, but lacks this Ca1 site and greatly changes its structure and position in a closed conformation. Lid2 forms a helical hairpin in an open conformation, but does not form it and covers the active site in a closed conformation. Based on these results, we discuss on the lid‐opening mechanism.