1aep: Difference between revisions

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[[Image:1aep.jpg|left|200px]]


{{Structure
==MOLECULAR STRUCTURE OF AN APOLIPOPROTEIN DETERMINED AT 2.5-ANGSTROMS RESOLUTION==
|PDB= 1aep |SIZE=350|CAPTION= <scene name='initialview01'>1aep</scene>, resolution 2.7&Aring;
<StructureSection load='1aep' size='340' side='right'caption='[[1aep]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND=
<table><tr><td colspan='2'>[[1aep]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Locusta_migratoria Locusta migratoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AEP FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aep OCA], [https://pdbe.org/1aep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aep RCSB], [https://www.ebi.ac.uk/pdbsum/1aep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aep ProSAT]</span></td></tr>
}}
</table>
 
== Function ==
'''MOLECULAR STRUCTURE OF AN APOLIPOPROTEIN DETERMINED AT 2.5-ANGSTROMS RESOLUTION'''
[https://www.uniprot.org/uniprot/APL3_LOCMI APL3_LOCMI] Assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It thus plays a critical role in the transport of lipids during flight in several species of insects.
 
__TOC__
 
</StructureSection>
==Overview==
[[Category: Large Structures]]
The three-dimensional structure of an apolipoprotein isolated from the African migratory locust Locusta migratoria has been determined by X-ray analysis to a resolution of 2.5 A. The overall molecular architecture of this protein consists of five long alpha-helices connected by short loops. As predicted from amino acid sequence analyses, these helices are distinctly amphiphilic with the hydrophobic residues pointing in toward the interior of the protein and the hydrophilic side chains facing outward. The molecule falls into the general category of up-and-down alpha-helical bundles as previously observed, for example, in cytochrome c'. Although the structure shows the presence of five long amphiphilic alpha-helices, the alpha-helical moment and hydrophobicity of the entire molecule fall into the range found for normal globular proteins. Thus, in order for the amphiphilic helices to play a role in the binding of the protein to a lipid surface, there must be a structural reorganization of the protein which exposes the hydrophobic interior to the lipid surface. The three-dimensional motif of this apolipoprotein is compatible with a model in which the molecule binds to the lipid surface via a relatively nonpolar end and then spreads on the surface in such a way as to cause the hydrophobic side chains of the helices to come in contact with the lipid surface, the charged and polar residues to remain in contact with water, and the overall helical motif of the protein to be maintained.
 
==About this Structure==
1AEP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Locusta_migratoria Locusta migratoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AEP OCA].  
 
==Reference==
Molecular structure of an apolipoprotein determined at 2.5-A resolution., Breiter DR, Kanost MR, Benning MM, Wesenberg G, Law JH, Wells MA, Rayment I, Holden HM, Biochemistry. 1991 Jan 22;30(3):603-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1988048 1988048]
[[Category: Locusta migratoria]]
[[Category: Locusta migratoria]]
[[Category: Single protein]]
[[Category: Holden H]]
[[Category: Holden, H.]]
[[Category: lipoprotein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:56:30 2008''

Latest revision as of 09:30, 7 February 2024

MOLECULAR STRUCTURE OF AN APOLIPOPROTEIN DETERMINED AT 2.5-ANGSTROMS RESOLUTIONMOLECULAR STRUCTURE OF AN APOLIPOPROTEIN DETERMINED AT 2.5-ANGSTROMS RESOLUTION

Structural highlights

1aep is a 1 chain structure with sequence from Locusta migratoria. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

APL3_LOCMI Assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It thus plays a critical role in the transport of lipids during flight in several species of insects.

1aep, resolution 2.70Å

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