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[[Image:1wbe.gif|left|200px]]<br /><applet load="1wbe" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1wbe, resolution 1.36&Aring;" />
'''X-RAY STRUCTURE OF BOVINE GLTP'''<br />


==Overview==
==X-ray structure of bovine GLTP==
Glycolipids participate in many important cellular processes and they are, bound and transferred with high specificity by glycolipid transfer protein, (GLTP). We have solved three different X-ray structures of bovine GLTP at, 1.4 angstroms, 1.6 angstroms and 1.8 angstroms resolution, all with a, bound fatty acid or glycolipid. The 1.4 angstroms structure resembles the, recently characterized apo-form of the human GLTP but the other two, structures represent an intermediate conformation of the apo-GLTPs and the, human lactosylceramide-bound GLTP structure. These novel structures give, insight into the mechanism of lipid binding and how GLTP may, conformationally adapt to different lipids. Furthermore, based on the, structural comparison of the GLTP structures and the three-dimensional, models of the related Podospora anserina HET-C2 and Arabidopsis thaliana, accelerated cell death protein, ACD11, we give structural explanations for, their specific lipid binding properties.
<StructureSection load='1wbe' size='340' side='right'caption='[[1wbe]], [[Resolution|resolution]] 1.36&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wbe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WBE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.36&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DKA:DECANOIC+ACID'>DKA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1wbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wbe OCA], [https://pdbe.org/1wbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wbe RCSB], [https://www.ebi.ac.uk/pdbsum/1wbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wbe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLTP_BOVIN GLTP_BOVIN] Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides.<ref>PMID:10671554</ref> <ref>PMID:16309699</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wb/1wbe_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1wbe ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycolipids participate in many important cellular processes and they are bound and transferred with high specificity by glycolipid transfer protein (GLTP). We have solved three different X-ray structures of bovine GLTP at 1.4 angstroms, 1.6 angstroms and 1.8 angstroms resolution, all with a bound fatty acid or glycolipid. The 1.4 angstroms structure resembles the recently characterized apo-form of the human GLTP but the other two structures represent an intermediate conformation of the apo-GLTPs and the human lactosylceramide-bound GLTP structure. These novel structures give insight into the mechanism of lipid binding and how GLTP may conformationally adapt to different lipids. Furthermore, based on the structural comparison of the GLTP structures and the three-dimensional models of the related Podospora anserina HET-C2 and Arabidopsis thaliana accelerated cell death protein, ACD11, we give structural explanations for their specific lipid binding properties.


==About this Structure==
Structural evidence for adaptive ligand binding of glycolipid transfer protein.,Airenne TT, Kidron H, Nymalm Y, Nylund M, West G, Mattjus P, Salminen TA J Mol Biol. 2006 Jan 13;355(2):224-36. Epub 2005 Nov 8. PMID:16309699<ref>PMID:16309699</ref>
1WBE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=DKA:'>DKA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WBE OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structural evidence for adaptive ligand binding of glycolipid transfer protein., Airenne TT, Kidron H, Nymalm Y, Nylund M, West G, Mattjus P, Salminen TA, J Mol Biol. 2006 Jan 13;355(2):224-36. Epub 2005 Nov 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16309699 16309699]
</div>
<div class="pdbe-citations 1wbe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Airenne, T.T.]]
[[Category: Airenne TT]]
[[Category: Kidron, H.]]
[[Category: Kidron H]]
[[Category: Mattjus, P.]]
[[Category: Mattjus P]]
[[Category: Nylund, M.]]
[[Category: Nylund M]]
[[Category: Nymalm, Y.]]
[[Category: Nymalm Y]]
[[Category: Salminen, T.A.]]
[[Category: Salminen TA]]
[[Category: West, G.]]
[[Category: West G]]
[[Category: DKA]]
[[Category: GOL]]
[[Category: acetylation]]
[[Category: glycolipid transfer]]
[[Category: lipid transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:21:24 2008''

Latest revision as of 16:27, 13 December 2023

X-ray structure of bovine GLTPX-ray structure of bovine GLTP

Structural highlights

1wbe is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.36Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLTP_BOVIN Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides.[1] [2]

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

Glycolipids participate in many important cellular processes and they are bound and transferred with high specificity by glycolipid transfer protein (GLTP). We have solved three different X-ray structures of bovine GLTP at 1.4 angstroms, 1.6 angstroms and 1.8 angstroms resolution, all with a bound fatty acid or glycolipid. The 1.4 angstroms structure resembles the recently characterized apo-form of the human GLTP but the other two structures represent an intermediate conformation of the apo-GLTPs and the human lactosylceramide-bound GLTP structure. These novel structures give insight into the mechanism of lipid binding and how GLTP may conformationally adapt to different lipids. Furthermore, based on the structural comparison of the GLTP structures and the three-dimensional models of the related Podospora anserina HET-C2 and Arabidopsis thaliana accelerated cell death protein, ACD11, we give structural explanations for their specific lipid binding properties.

Structural evidence for adaptive ligand binding of glycolipid transfer protein.,Airenne TT, Kidron H, Nymalm Y, Nylund M, West G, Mattjus P, Salminen TA J Mol Biol. 2006 Jan 13;355(2):224-36. Epub 2005 Nov 8. PMID:16309699[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Lin X, Mattjus P, Pike HM, Windebank AJ, Brown RE. Cloning and expression of glycolipid transfer protein from bovine and porcine brain. J Biol Chem. 2000 Feb 18;275(7):5104-10. PMID:10671554
  2. ↑ Airenne TT, Kidron H, Nymalm Y, Nylund M, West G, Mattjus P, Salminen TA. Structural evidence for adaptive ligand binding of glycolipid transfer protein. J Mol Biol. 2006 Jan 13;355(2):224-36. Epub 2005 Nov 8. PMID:16309699 doi:10.1016/j.jmb.2005.10.031
  3. ↑ Airenne TT, Kidron H, Nymalm Y, Nylund M, West G, Mattjus P, Salminen TA. Structural evidence for adaptive ligand binding of glycolipid transfer protein. J Mol Biol. 2006 Jan 13;355(2):224-36. Epub 2005 Nov 8. PMID:16309699 doi:10.1016/j.jmb.2005.10.031

1wbe, resolution 1.36Å

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