[feed] Atom [feed] RSS 1.0 [feed] RSS 2.0

Madni, Zaid Kamal and Tripathi, Sunil Kumar and Salunke, Dinakar M. (2019) Structural insights into the lipid transfer mechanism of a non‐specific lipid transfer protein. The Plant Journal. ISSN 0960-7412

[img] Text
Madni_The Plant Journal_2019.pdf
Restricted to Registered users only

Download (5Mb) | Request a copy

Abstract

The non-specific lipid transfer proteins (nsLTPs) are multifunctional seed proteins engaged in several differ-ent physiological processes. The nsLTPs are stabilized by four disulfide bonds and exhibit a characteristichydrophobic cavity, which is the primary lipid binding site. While these proteins are known to transfer lipidsbetween membranes, the mechanism of lipid transfer has remained elusive. Four crystal structures of nsLTPfromSolanum melongena, one in the apo-state and three myristic acid bound states were determined.Among the three lipid bound states, two lipid molecules were bound on the nsLTP surface at different posi-tions and one was inside the cavity. The lipid-dependent conformational changes leading to opening of thecavity were revealed based on structural and spectroscopic data. The surface-bound lipid represented a tran-sient intermediate state and the lipid ultimately moved inside the cavity through the cavity gate as revealedby molecular dynamics simulations. Two critical residues in the loop regions played possible ‘gating’ role inthe opening and closing of the cavity. Antifungal activity and membrane permeabilization effect of nsLTPagainstFusarium oxysporumsuggested that it could possibly involve in bleaching out the lipids. Collec-tively, these studies support a model of lipid transfer mechanism by nsLTP via intermediate states.

Item Type: Article
Subjects: Biomedical Science
Biochemical and Biophysical Sciences
Depositing User: RCB Library
Date Deposited: 17 Mar 2020 08:15
Last Modified: 17 Mar 2020 08:15
URI: http://rcb.sciencecentral.in/id/eprint/186

Actions (login required)

View Item View Item