1TUK: Crystal Structure Of Liganded Type 2 Non Specific Lipid Transfer Protein From Wheat

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.
PDB ID: 1TUKDownload
MMDB ID: 32252
PDB Deposition Date: 2004/6/25
Updated in MMDB: 2016/12
Experimental Method:
x-ray diffraction
Resolution: 1.12  Å
Source Organism:
Similar Structures:
Biological Unit for 1TUK: monomeric; determined by author
Molecular Components in 1TUK
Label Count Molecule
Protein (1 molecule)
Nonspecific Lipid-transfer Protein 2G
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB