1fk6
From Proteopedia
(New page: 200px<br /><applet load="1fk6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fk6, resolution 1.9Å" /> '''STRUCTURAL BASIS OF N...) |
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| - | [[Image:1fk6.jpg|left|200px]]<br /><applet load="1fk6" size=" | + | [[Image:1fk6.jpg|left|200px]]<br /><applet load="1fk6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fk6, resolution 1.9Å" /> | caption="1fk6, resolution 1.9Å" /> | ||
'''STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH ALPHA-LINOLENIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY'''<br /> | '''STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH ALPHA-LINOLENIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Non-specific lipid-transfer proteins (nsLTPs) are involved in the movement | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1FK6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with LNL and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1FK6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with <scene name='pdbligand=LNL:'>LNL</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FK6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Zea mays]] | [[Category: Zea mays]] | ||
| - | [[Category: Han, G | + | [[Category: Han, G W.]] |
| - | [[Category: Lee, J | + | [[Category: Lee, J Y.]] |
| - | [[Category: Shin, D | + | [[Category: Shin, D H.]] |
| - | [[Category: Song, H | + | [[Category: Song, H K.]] |
| - | [[Category: Suh, S | + | [[Category: Suh, S W.]] |
[[Category: FMT]] | [[Category: FMT]] | ||
[[Category: LNL]] | [[Category: LNL]] | ||
[[Category: protein-lipid complex]] | [[Category: protein-lipid complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:30 2008'' |
Revision as of 10:39, 21 February 2008
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STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH ALPHA-LINOLENIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY
Overview
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.
About this Structure
1FK6 is a Single protein structure of sequence from Zea mays with and as ligands. 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
Page seeded by OCA on Thu Feb 21 12:39:30 2008
Categories: Single protein | Zea mays | Han, G W. | Lee, J Y. | Shin, D H. | Song, H K. | Suh, S W. | FMT | LNL | Protein-lipid complex
