Crystal structure of a family I.3 lipase from  Pseudomonas  sp. MIS38 in a closed conformation | Zendy

Angkawidjaja Clement | Zendy; You Dong-ju | Zendy; Matsumura Hiroyoshi | Zendy; Kuwahara Katsumasa | Zendy; Koga Yuichi | Zendy; Takano Kazufumi | Zendy; Kanaya Shigenori | Zendy

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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.

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