Modeling of solvent-dependent conformational transitions in Burkholderia cepacia lipase.

ABSTRACT:

Background

The characteristic of most lipases is the interfacial activation at a lipid interface or in non-polar solvents. Interfacial activation is linked to a large conformational change of a lid, from a closed to an open conformation which makes the active site accessible for substrates. While for many lipases crystal structures of the closed and open conformation have been determined, the pathway of the conformational transition and possible bottlenecks are unknown. Therefore, molecular dynamics simulations of a closed homology model and an open crystal structure of Burkholderia cepacia lipase in water and toluene were performed to investigate the influence of solvents on structure, dynamics, and the conformational transition of the lid.

Results

The conformational transi

SUBMITTER: Trodler P 

PROVIDER: S-EPMC2695465 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature