1tuk
From Proteopedia
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|PDB= 1tuk |SIZE=350|CAPTION= <scene name='initialview01'>1tuk</scene>, resolution 1.12Å | |PDB= 1tuk |SIZE=350|CAPTION= <scene name='initialview01'>1tuk</scene>, resolution 1.12Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene> | + | |LIGAND= <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PGM:1-MYRISTOYL-2-HYDROXY-SN-GLYCERO-3-[PHOSPHO-RAC-(1-GLYCEROL)]'>PGM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1n89|1N89]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tuk OCA], [http://www.ebi.ac.uk/pdbsum/1tuk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tuk RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Lamotte, F De.]] | [[Category: Lamotte, F De.]] | ||
[[Category: Pons, J L.]] | [[Category: Pons, J L.]] | ||
| - | [[Category: IOD]] | ||
| - | [[Category: PGM]] | ||
[[Category: lipid transfer protein]] | [[Category: lipid transfer protein]] | ||
[[Category: ns-ltp2]] | [[Category: ns-ltp2]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:01:15 2008'' |
Revision as of 21:01, 30 March 2008
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| , resolution 1.12Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1N89
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal stucture of liganted type 2 non specific lipid transfer protein from wheat
Overview
In plants, a family of ubiquitous proteins named non-specific lipid-transfer proteins (ns-LTPs) facilitates the transfer of fatty acids, phospholipids and steroids between membranes. Recent data suggest that these secreted proteins play a key role in the formation of cuticular wax layers and in defence mechanisms against pathogens. In this study, X-ray crystallography has been used to examine the structural details of the interaction between a wheat type 2 ns-LTP and a lipid, L-alpha-palmitoyl-phosphatidyl glycerol. This crystal structure was solved ab initio at 1.12 A resolution by direct methods. The typical alpha-helical bundle fold of this protein is maintained by four disulfide bridges and delineates two hydrophobic cavities. The inner surface of the main cavity is lined by non-polar residues that provide a hydrophobic environment for the palmitoyl moiety of the lipid. The head-group region of this lipid protrudes from the surface and makes several polar interactions with a conserved patch of basic residues at the entrance of the pocket. The alkyl chain of a second lipid is bound within an adjacent smaller cavity. The structure shows that binding of the lipid tails to the protein involves extensive hydrophobic interactions.
About this Structure
1TUK is a Single protein structure of sequence from Triticum aestivum. Full crystallographic information is available from OCA.
Reference
Structure of a liganded type 2 non-specific lipid-transfer protein from wheat and the molecular basis of lipid binding., Hoh F, Pons JL, Gautier MF, de Lamotte F, Dumas C, Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):397-406. Epub 2005, Mar 24. PMID:15805594
Page seeded by OCA on Mon Mar 31 00:01:15 2008
