title: Evidence of a double-lid movement in Pseudomonas aeruginosa lipase: insights from molecular dynamics simulations.
abstract: Pseudomonas aeruginosa lipase is a 29-kDa protein that, following the determination of its crystal structure, was postulated to have a lid that stretched between residues 125 and 148. In this paper, using molecular dynamics simulations, we propose that there exists, in addition to the above-mentioned lid, a novel second lid in this lipase. We further show that the second lid, covering residues 210-222, acts as a triggering lid for the movement of the first. We also investigate the role of hydrophobicity in the movement of the lids and show that two residues, Phe214 and Ala217, play important roles in lid movement. To our knowledge, this is the first time that a double-lid movement of the type described in our manuscript has been presented to the scientific community. This work also elucidates the interplay of hydrophobic interactions in the dynamics, and hence the function, of an enzyme.
authors.affiliation: Centre for Biotechnology, Anna University, Chennai, India.
authors.forename: Subbulakshmi Latha
authors.initials: SL
authors.lastname: Cherukuvada
authors.forename: Aswin Sai Narain
authors.initials: AS
authors.lastname: Seshasayee
authors.forename: Krishnan
authors.initials: K
authors.lastname: Raghunathan
authors.forename: Sharmila
authors.initials: S
authors.lastname: Anishetty
authors.forename: Gautam
authors.initials: G
authors.lastname: Pennathur
mesh_terms: D003198:Computer Simulation; D057927:Hydrophobic and Hydrophilic Interactions; D008049:Lipase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D009068:Movement; D009154:Mutation / Q000235:genetics; D020836:Protein Structure, Quaternary; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000235:genetics
chemical_list: D008049:Lipase