Open Access3‐D structure modelling of the Staphylococcus simulans lipase: conformational changes, substrate specificity and novel structural features
Author(s) -
Frikha Fakher,
Ladjimi Moncef,
Gargouri Youssef,
Miled Nabil
Publication year - 2008
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2008.01279.x
Subject(s) - lipase , molecular dynamics , hinge , substrate (aquarium) , chemistry , crystallography , active site , flexibility (engineering) , stereochemistry , biophysics , biology , enzyme , physics , biochemistry , computational chemistry , classical mechanics , ecology , statistics , mathematics
We have modelled, using the CHARMM27 energy force field, the structures of closed and open forms of Staphylococcus simulans lipase (SSL) on the basis of the crystal structures of Bacillus stearothermophilus and Staphylococcus hyicus lipases, respectively. The models suggested the presence of a main lid and a second lid that may act with the former as a double door to control the access to the active site. Superimposition of both closed and open forms of SSL allowed us to determine the hinge regions allowing the movements of the main and the second lid upon lipase activation. The flexibility of these hinge regions was checked by molecular dynamics simulations. The SSL models also allowed us to identify key residues involved in binding substrates, calcium or zinc ions.