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Structural Basis of Non-specific Lipid Ginding in Maize Lipid-transfer Protein Complexes Revealed by High-resolution X-ray Crystallography

Authors
Gye Won HanJae Young LeeHyun Kyu SongChangsoo ChangKyeongsik MinJinho MoonDong Hae ShinMary L KopkaMichael R SawayaHanna S YuanJungwoo ChoeDori LimKim, Doo HunHee Jung MoonSe Won Suh
Issue Date
Apr-2001
Publisher
Academic Press
Citation
Journal of Molecular Biology, v.308, no.2, pp 263 - 278
Pages
16
Journal Title
Journal of Molecular Biology
Volume
308
Number
2
Start Page
263
End Page
278
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/159133
DOI
10.1006/jmbi.2001.4559
ISSN
0022-2836
1089-8638
Abstract
Non-specific lipid-transfer proteins (nsLTPs) are involved in the movement of phospholipids, glycolipids, fatty acids, and steroids between membranes. Several structures of plant nsLTPs have been determined both by X-ray crystallography and nuclear magnetic resonance. However, the detailed structural basis of the non-specific binding of hydrophobic ligands by nsLTPs is still poorly understood. In order to gain a better understanding of the structural basis of the non-specific binding of hydrophobic ligands by nsLTPs and to investigate the plasticity of the fatty acid binding cavity in nsLTPs, seven high-resolution (between 1.3 Å and 1.9 Å) crystal structures have been determined. These depict the nsLTP from maize seedlings in complex with an array of fatty acids. A detailed comparison of the structures of maize nsLTP in complex with various ligands reveals a new binding mode in an nsLTP-oleate complex which has not been seen before. Furthermore, in the caprate complex, the ligand binds to the protein cavity in two orientations with equal occupancy. The volume of the hydrophobic cavity in the nsLTP from maize shows some variation depending on the size of the bound ligands. The structural plasticity of the ligand binding cavity and the predominant involvement of non-specific van der Waals interactions with the hydrophobic tail of the ligands provide a structural explanation for the non-specificity of maize nsLTP. The hydrophobic cavity accommodates various ligands from C10 to C18. The C18:1 ricinoleate with its hydroxyl group hydrogen bonding to Ala68 possibly mimics cutin monomer binding which is of biological importance. Some of the myristate binding sites in human serum albumin resemble the maize nsLTP, implying the importance of a helical bundle in accommodating the non-specific binding of fatty acids.
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