1lsh | pdb_00001lsh

LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN

spinqualitylabelsall models 1lsh, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1lsh is a 2 chain structure with sequence from Ichthyomyzon unicuspis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PLD, UPL NonStd Res: PCA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [VIT_ICHUN] Precursor of the major egg-yolk proteins that are sources of nutrients during early development of oviparous organisms. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Lipid-protein interactions in lipovitellin.,Thompson JR, Banaszak LJ Biochemistry. 2002 Jul 30;41(30):9398-409. PMID:12135361 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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