2bv7: Difference between revisions
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==Crystal structure of GLTP with bound GM3== | |||
<StructureSection load='2bv7' size='340' side='right' caption='[[2bv7]], [[Resolution|resolution]] 1.79Å' scene=''> | <StructureSection load='2bv7' size='340' side='right' caption='[[2bv7]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GM3:N-{1-[(HEXOPYRANOSYLOXY)METHYL]-2-HYDROXYNONADECYL}TETRACOSANAMIDE'>GM3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GM3:N-{1-[(HEXOPYRANOSYLOXY)METHYL]-2-HYDROXYNONADECYL}TETRACOSANAMIDE'>GM3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tfj|1tfj]], [[1wbe|1wbe]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tfj|1tfj]], [[1wbe|1wbe]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bv7 OCA], [http://pdbe.org/2bv7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bv7 RCSB], [http://www.ebi.ac.uk/pdbsum/2bv7 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bv7 OCA], [http://pdbe.org/2bv7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bv7 RCSB], [http://www.ebi.ac.uk/pdbsum/2bv7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bv7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bv/2bv7_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bv/2bv7_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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[[Category: Salminen, T A]] | [[Category: Salminen, T A]] | ||
[[Category: West, G]] | [[Category: West, G]] | ||
[[Category: Acetylation]] | |||
[[Category: Glycolipid]] | [[Category: Glycolipid]] | ||
[[Category: Glycolipid transfer protein]] | [[Category: Glycolipid transfer protein]] | ||
Revision as of 09:32, 16 May 2018
Crystal structure of GLTP with bound GM3Crystal structure of GLTP with bound GM3
Structural highlights
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 PubMedGlycolipids 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
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