1wbe: Difference between revisions

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-[[Image:1wbe.png|left|200px]]
-<!--
+==X-ray structure of bovine GLTP==
-The line below this paragraph, containing "STRUCTURE_1wbe", creates the "Structure Box" on the page.
+<StructureSection load='1wbe' size='340' side='right'caption='[[1wbe]], [[Resolution|resolution]] 1.36&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
-{{STRUCTURE_1wbe|  PDB=1wbe  |  SCENE=  }}
+<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.
-===X-RAY STRUCTURE OF BOVINE GLTP===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_16309699}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1wbe" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16309699 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16309699}}
+__TOC__
+</StructureSection>
-==About this Structure==
-[[1wbe]] is a 1 chain structure with 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=1WBE OCA].
-==Reference==
-<ref group="xtra">PMID:16309699</ref><ref group="xtra">PMID:15039559</ref><references group="xtra"/>
 [[Category: Bos taurus]]
-[[Category: Airenne, T T.]]
+[[Category: Large Structures]]
-[[Category: Kidron, H.]]
+[[Category: Airenne TT]]
-[[Category: Mattjus, P.]]
+[[Category: Kidron H]]
-[[Category: Nylund, M.]]
+[[Category: Mattjus P]]
-[[Category: Nymalm, Y.]]
+[[Category: Nylund M]]
-[[Category: Salminen, T A.]]
+[[Category: Nymalm Y]]
-[[Category: West, G.]]
+[[Category: Salminen TA]]
-[[Category: Acetylation]]
+[[Category: West G]]
-[[Category: Glycolipid transfer]]
-[[Category: Glycolipid transfer protein]]
-[[Category: Lipid transport]]