1lsh
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1lsh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ichthyomyzon_unicuspis Ichthyomyzon unicuspis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LSH FirstGlance]. <br> | <table><tr><td colspan='2'>[[1lsh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ichthyomyzon_unicuspis Ichthyomyzon unicuspis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LSH FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PLD:DIUNDECYL+PHOSPHATIDYL+CHOLINE'>PLD</scene>, <scene name='pdbligand=UPL:UNKNOWN+BRANCHED+FRAGMENT+OF+PHOSPHOLIPID'>UPL</scene></td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lsh OCA], [https://pdbe.org/1lsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lsh RCSB], [https://www.ebi.ac.uk/pdbsum/1lsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lsh ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lsh OCA], [https://pdbe.org/1lsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lsh RCSB], [https://www.ebi.ac.uk/pdbsum/1lsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lsh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/VIT_ICHUN VIT_ICHUN] Precursor of the major egg-yolk proteins that are sources of nutrients during early development of oviparous organisms. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 20: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lsh ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lsh ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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<ref>PMID:12135361</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1lsh" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ichthyomyzon unicuspis]] | [[Category: Ichthyomyzon unicuspis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Banaszak | + | [[Category: Banaszak LJ]] |
| - | [[Category: Thompson | + | [[Category: Thompson JR]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Revision as of 06:06, 3 April 2024
LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN
| |||||||||||
