This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4gh0

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:03, 5 August 2016

Crystal structure of D48V mutant of human GLTP bound with 12:0 monosulfatide

Structural highlights

4gh0 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	3s0i, 4ghp, 4ghs
Gene:	GLTP (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GLTP_HUMAN] 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] ^[3] ^[4]

Publication Abstract from PubMed

Human glycolipid transfer protein (hsGLTP) forms the prototypical GLTP fold and is characterized by a broad transfer selectivity for glycosphingolipids (GSLs). The GLTP mutation D48V near the `portal entrance' of the glycolipid binding site has recently been shown to enhance selectivity for sulfatides (SFs) containing a long acyl chain. Here, nine novel crystal structures of hsGLTP and the SF-selective mutant complexed with short-acyl-chain monoSF and diSF in different crystal forms are reported in order to elucidate the potential functional roles of lipid-mediated homodimerization. In all crystal forms, the hsGLTP-SF complexes displayed homodimeric structures supported by similarly organized intermolecular interactions. The dimerization interface always involved the lipid sphingosine chain, the protein C-terminus (C-end) and alpha-helices 6 and 2, but the D48V mutant displayed a `locked' dimer conformation compared with the hinge-like flexibility of wild-type dimers. Differences in contact angles, areas and residues at the dimer interfaces in the `flexible' and `locked' dimers revealed a potentially important role of the dimeric structure in the C-end conformation of hsGLTP and in the precise positioning of the key residue of the glycolipid recognition centre, His140. DeltaY207 and DeltaC-end deletion mutants, in which the C-end is shifted or truncated, showed an almost complete loss of transfer activity. The new structural insights suggest that ligand-dependent reversible dimerization plays a role in the function of human GLTP.

Structural insights into lipid-dependent reversible dimerization of human GLTP.,Samygina VR, Ochoa-Lizarralde B, Popov AN, Cabo-Bilbao A, Goni-de-Cerio F, Molotkovsky JG, Patel DJ, Brown RE, Malinina L Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):603-16. doi:, 10.1107/S0907444913000024. Epub 2013 Mar 14. PMID:23519669^[5]

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

References

↑ Zou X, Chung T, Lin X, Malakhova ML, Pike HM, Brown RE. Human glycolipid transfer protein (GLTP) genes: organization, transcriptional status and evolution. BMC Genomics. 2008 Feb 8;9:72. PMID:18261224 doi:1471-2164-9-72
↑ Rao CS, Lin X, Pike HM, Molotkovsky JG, Brown RE. Glycolipid transfer protein mediated transfer of glycosphingolipids between membranes: a model for action based on kinetic and thermodynamic analyses. Biochemistry. 2004 Nov 2;43(43):13805-15. PMID:15504043 doi:10.1021/bi0492197
↑ Tuuf J, Mattjus P. Human glycolipid transfer protein--intracellular localization and effects on the sphingolipid synthesis. Biochim Biophys Acta. 2007 Nov;1771(11):1353-63. Epub 2007 Sep 21. PMID:17980653 doi:S1388-1981(07)00196-5
↑ Malinina L, Malakhova ML, Teplov A, Brown RE, Patel DJ. Structural basis for glycosphingolipid transfer specificity. Nature. 2004 Aug 26;430(7003):1048-53. PMID:15329726 doi:10.1038/nature02856
↑ Samygina VR, Ochoa-Lizarralde B, Popov AN, Cabo-Bilbao A, Goni-de-Cerio F, Molotkovsky JG, Patel DJ, Brown RE, Malinina L. Structural insights into lipid-dependent reversible dimerization of human GLTP. Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):603-16. doi:, 10.1107/S0907444913000024. Epub 2013 Mar 14. PMID:23519669 doi:10.1107/S0907444913000024

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4gh0"

@@ Line 1: / Line 1: @@
 ==Crystal structure of D48V mutant of human GLTP bound with 12:0 monosulfatide==
 <StructureSection load='4gh0' size='340' side='right' caption='[[4gh0]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4gh0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GH0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4gh0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GH0 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EIS:N-{(2S,3R,4E)-3-HYDROXY-1-[(3-O-SULFO-BETA-D-GALACTOPYRANOSYL)OXY]OCTADEC-4-EN-2-YL}DODECANAMIDE'>EIS</scene>, <scene name='pdbligand=MYS:PENTADECANE'>MYS</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3s0i|3s0i]], [[4ghp|4ghp]], [[4ghs|4ghs]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLTP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLTP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4gh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gh0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gh0 RCSB], [http://www.ebi.ac.uk/pdbsum/4gh0 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=4gh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gh0 OCA], [http://pdbe.org/4gh0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gh0 RCSB], [http://www.ebi.ac.uk/pdbsum/4gh0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gh0 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4gh0" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Cabo-Bilbao, A]]
 [[Category: Malinina, L]]

4gh0

From Proteopedia

Revision as of 10:03, 5 August 2016

Crystal structure of D48V mutant of human GLTP bound with 12:0 monosulfatide

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox