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[[Image:1tfj.gif|left|200px]]


{{Structure
==Crystal structure of Bovine Glycolipid transfer protein in complex with a fatty acid==
|PDB= 1tfj |SIZE=350|CAPTION= <scene name='initialview01'>1tfj</scene>, resolution 1.61&Aring;
<StructureSection load='1tfj' size='340' side='right'caption='[[1tfj]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DKA:DECANOIC+ACID'>DKA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
<table><tr><td colspan='2'>[[1tfj]] 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=1TFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TFJ 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]] 1.61&#8491;</td></tr>
|GENE= GLTP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DKA:DECANOIC+ACID'>DKA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tfj OCA], [https://pdbe.org/1tfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tfj RCSB], [https://www.ebi.ac.uk/pdbsum/1tfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tfj ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tfj OCA], [http://www.ebi.ac.uk/pdbsum/1tfj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tfj RCSB]</span>
== 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 ==
'''Crystal structure of Bovine Glycolipid transfer protein in complex with a fatty acid'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tf/1tfj_consurf.spt"</scriptWhenChecked>
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.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1TFJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFJ OCA].  
</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=1tfj ConSurf].
 
<div style="clear:both"></div>
==Reference==
== References ==
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://www.ncbi.nlm.nih.gov/pubmed/16309699 16309699]
<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: Nymalm, Y.]]
[[Category: Nymalm Y]]
[[Category: Salminen, T A.]]
[[Category: Salminen TA]]
[[Category: West, G.]]
[[Category: West G]]
[[Category: glycolipid]]
[[Category: lipid transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:24 2008''

Latest revision as of 11:39, 14 February 2024

Crystal structure of Bovine Glycolipid transfer protein in complex with a fatty acidCrystal structure of Bovine Glycolipid transfer protein in complex with a fatty acid

Structural highlights

1tfj 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 1.61Å
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.

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

1tfj, resolution 1.61Å

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