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1fk2

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{{STRUCTURE_1fk2| PDB=1fk2 | SCENE= }}
{{STRUCTURE_1fk2| PDB=1fk2 | SCENE= }}
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'''STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH MYRISTIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY'''
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===STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH MYRISTIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_11327766}}
==About this Structure==
==About this Structure==
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[[Category: Suh, S W.]]
[[Category: Suh, S W.]]
[[Category: Protein-lipid complex]]
[[Category: Protein-lipid complex]]
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Revision as of 00:23, 1 July 2008

Image:1fk2.png

Template:STRUCTURE 1fk2

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

Template:ABSTRACT PUBMED 11327766

About this Structure

1FK2 is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.

Reference

Structural basis of non-specific lipid binding in maize lipid-transfer protein complexes revealed by high-resolution X-ray crystallography., Han GW, Lee JY, Song HK, Chang C, Min K, Moon J, Shin DH, Kopka ML, Sawaya MR, Yuan HS, Kim TD, Choe J, Lim D, Moon HJ, Suh SW, J Mol Biol. 2001 Apr 27;308(2):263-78. PMID:11327766

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