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3gsh

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Revision as of 07:11, 1 November 2017

Three-dimensional structure of a post translational modified barley LTP1

Structural highlights

3gsh is a 2 chain structure with sequence from Hordeum vulgare. This structure supersedes the now removed PDB entry 3cee. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	1mid
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NLTP1_HORVU] Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.

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

The barley lipid transfer protein (LTP1) adducted by an alpha-ketol, (9-hydroxy-10-oxo-12(Z)-octadecenoic acid) exhibits an unexpected high lipid transfer activity. The crystal structure of this oxylipin-adducted LTP1, (LTP1b) was determined at 1.8A resolution. The covalently bound oxylipin was partly exposed at the surface of the protein and partly buried within the hydrophobic cavity. The structure of the oxylipidated LTP1 emphasizes the unique plasticity of the hydrophobic cavity of these plant lipid-binding proteins when compared to the other members of the family. The plasticity of the hydrophobic cavity and increase of its surface hydrophobicity induced by the oxylipin account for the improvement of the lipid transfer activity of LTP1b. These observations open new perspectives to explore the different biological functions of LTPs, including their allergenic properties.

The crystal structure of oxylipin-conjugated barley LTP1 highlights the unique plasticity of the hydrophobic cavity of these plant lipid-binding proteins.,Bakan B, Hamberg M, Larue V, Prange T, Marion D, Lascombe MB Biochem Biophys Res Commun. 2009 Dec 18;390(3):780-5. Epub 2009 Oct 20. PMID:19836358^[1]

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

References

↑ Bakan B, Hamberg M, Larue V, Prange T, Marion D, Lascombe MB. The crystal structure of oxylipin-conjugated barley LTP1 highlights the unique plasticity of the hydrophobic cavity of these plant lipid-binding proteins. Biochem Biophys Res Commun. 2009 Dec 18;390(3):780-5. Epub 2009 Oct 20. PMID:19836358 doi:10.1016/j.bbrc.2009.10.049

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3gsh"

@@ Line 1: / Line 1: @@
 ==Three-dimensional structure of a post translational modified barley LTP1==
 <StructureSection load='3gsh' size='340' side='right' caption='[[3gsh]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASY:(12E)-10-OXOOCTADEC-12-ENOIC+ACID'>ASY</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TFA:TRIFLUOROACETIC+ACID'>TFA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mid|1mid]]</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=3gsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gsh OCA], [http://pdbe.org/3gsh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gsh RCSB], [http://www.ebi.ac.uk/pdbsum/3gsh 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=3gsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gsh OCA], [http://pdbe.org/3gsh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gsh RCSB], [http://www.ebi.ac.uk/pdbsum/3gsh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gsh ProSAT]</span></td></tr>
 </table>
 == Function ==

3gsh

From Proteopedia

Revision as of 07:11, 1 November 2017

Three-dimensional structure of a post translational modified barley LTP1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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