1lsh
From Proteopedia
(New page: 200px<br /><applet load="1lsh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lsh, resolution 1.90Å" /> '''LIPID-PROTEIN INTERA...) |
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| - | [[Image:1lsh.gif|left|200px]]<br /><applet load="1lsh" size=" | + | [[Image:1lsh.gif|left|200px]]<br /><applet load="1lsh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lsh, resolution 1.90Å" /> | caption="1lsh, resolution 1.90Å" /> | ||
'''LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN'''<br /> | '''LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The refined molecular structure of lipovitellin is described using | + | The refined molecular structure of lipovitellin is described using synchrotron cryocrystallographic data to 1.9 A resolution. Lipovitellin is the predominant lipoprotein found in the yolk of egg-laying animals and is involved in lipid and metal storage. It is thought to be related in amino acid sequence to segments of apolipoprotein B and the microsomal transfer protein responsible for the assembly of low-density lipoproteins. Lipovitellin contains a heterogeneous mixture of about 16% (w/w) noncovalently bound lipid, mostly phospholipid. Previous X-ray structural studies at ambient temperature described several different protein domains including a large cavity in each subunit of the dimeric protein. The cavity was free of any visible electron density for lipid molecules at room temperature, suggesting that only dynamic interactions exist with the protein. An important result from this crystallographic study at 100 K is the appearance of some bound ordered lipid along the walls of the binding cavity. The precise identification of the lipid type is difficult because of discontinuities in the electron density. Nonetheless, the conformations of 7 phospholipids and 43 segments of hydrocarbon chains greater than 5 atoms in length have been discovered. The conformations of the bound lipid and the interactions between protein and lipid provide insights into the factors governing lipoprotein formation. |
==About this Structure== | ==About this Structure== | ||
| - | 1LSH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Ichthyomyzon_unicuspis Ichthyomyzon unicuspis] with PLD and UPL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1LSH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Ichthyomyzon_unicuspis Ichthyomyzon unicuspis] with <scene name='pdbligand=PLD:'>PLD</scene> and <scene name='pdbligand=UPL:'>UPL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LSH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ichthyomyzon unicuspis]] | [[Category: Ichthyomyzon unicuspis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Banaszak, L | + | [[Category: Banaszak, L J.]] |
| - | [[Category: Thompson, J | + | [[Category: Thompson, J R.]] |
[[Category: PLD]] | [[Category: PLD]] | ||
[[Category: UPL]] | [[Category: UPL]] | ||
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[[Category: vitellogenin]] | [[Category: vitellogenin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:58 2008'' |
Revision as of 11:47, 21 February 2008
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LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN
Overview
The refined molecular structure of lipovitellin is described using synchrotron cryocrystallographic data to 1.9 A resolution. Lipovitellin is the predominant lipoprotein found in the yolk of egg-laying animals and is involved in lipid and metal storage. It is thought to be related in amino acid sequence to segments of apolipoprotein B and the microsomal transfer protein responsible for the assembly of low-density lipoproteins. Lipovitellin contains a heterogeneous mixture of about 16% (w/w) noncovalently bound lipid, mostly phospholipid. Previous X-ray structural studies at ambient temperature described several different protein domains including a large cavity in each subunit of the dimeric protein. The cavity was free of any visible electron density for lipid molecules at room temperature, suggesting that only dynamic interactions exist with the protein. An important result from this crystallographic study at 100 K is the appearance of some bound ordered lipid along the walls of the binding cavity. The precise identification of the lipid type is difficult because of discontinuities in the electron density. Nonetheless, the conformations of 7 phospholipids and 43 segments of hydrocarbon chains greater than 5 atoms in length have been discovered. The conformations of the bound lipid and the interactions between protein and lipid provide insights into the factors governing lipoprotein formation.
About this Structure
1LSH is a Protein complex structure of sequences from Ichthyomyzon unicuspis with and as ligands. Full crystallographic information is available from OCA.
Reference
Lipid-protein interactions in lipovitellin., Thompson JR, Banaszak LJ, Biochemistry. 2002 Jul 30;41(30):9398-409. PMID:12135361
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