1FK0

STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH CAPRIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY

Summary for 1FK0

• Entry DOI: 10.2210/pdb1fk0/pdb
• Related: 1FK1 1FK2 1FK3 1FK4 1FK5 1FK6 1FK7 1MZL 1MZM
• Descriptor: NONSPECIFIC LIPID-TRANSFER PROTEIN, DECANOIC ACID, FORMIC ACID, ... (4 entities in total)
• Functional Keywords: protein-lipid complex, lipid transport
• Biological source: Zea mays
• Total number of polymer chains: 1
• Total formula weight: 9326.48

Authors

Han, G.W.,Lee, J.Y.,Song, H.K.,Shin, D.H.,Suh, S.W. (deposition date: 2000-08-08, release date: 2001-06-06, Last modification date: 2023-10-25)

Primary citation

Han, G.W.,Lee, J.Y.,Song, H.K.,Chang, C.,Min, K.,Moon, J.,Shin, D.H.,Kopka, M.L.,Sawaya, M.R.,Yuan, H.S.,Kim, T.D.,Choe, J.,Lim, D.,Moon, H.J.,Suh, S.W.
Structural basis of non-specific lipid binding in maize lipid-transfer protein complexes revealed by high-resolution X-ray crystallography.
J.Mol.Biol., 308:263-278, 2001

PubMed 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 A and 1.9 A) 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.

PubMed: 11327766
DOI: 10.1006/jmbi.2001.4559

Experimental method

X-RAY DIFFRACTION (1.8 Å)