PDBsum entry 1l6h

Lipid transport

PDB id: 1l6h

Contents

Protein chain

69 a.a. *

* Residue conservation analysis

PDB id:

1l6h

Name:

Lipid transport

Title:

Solution structure of plant nsltp2 purified from rice (oryza sativa)

Structure:

Non-specific lipid transfer protein. Chain: a. Synonym: ltp2

Source:

Oryza sativa. Rice. Organism_taxid: 4530

NMR struc:

1 models

Authors:

D.Samuel,P.-C.Lyu

Key ref:

D.Samuel et al. (2002). Solution structure of plant nonspecific lipid transfer protein-2 from rice (Oryza sativa). J Biol Chem, 277, 35267-35273. PubMed id: 12011089 DOI: 10.1074/jbc.M203113200

Date:

11-Mar-02 Release date: 02-Oct-02

Protein chain

Q10ST8  (NLTPX_ORYSJ) -  Non-specific lipid-transfer protein 2 from Oryza sativa subsp. japonica

Seq: 96 a.a.

Struc: 69 a.a.

DOI no: 10.1074/jbc.M203113200

J Biol Chem 277:35267-35273 (2002)

PubMed id: 12011089

Solution structure of plant nonspecific lipid transfer protein-2 from rice (Oryza sativa).

D.Samuel, Y.J.Liu, C.S.Cheng, P.C.Lyu.

ABSTRACT

The three-dimensional structure of rice nonspecific lipid transfer protein (nsLTP2) has been solved for the first time. The structure of nsLTP2 was obtained using 813 distance constraints, 30 hydrogen bond constraints, and 19 dihedral angle constraints. Fifteen of the 50 random simulated annealing structures satisfied all of the constraints and possessed good nonbonded contacts. The novel three-dimensional fold of rice nsLTP2 contains a triangular hydrophobic cavity formed by three prominent helices. The four disulfide bonds required for stabilization of the nsLTP2 structure show a different pattern of cysteine pairing compared with nsLTP1. The C terminus of the protein is very flexible and forms a cap over the hydrophobic cavity. Molecular modeling studies suggested that the hydrophobic cavity could accommodate large molecules with rigid structures, such as sterols. The positively charged residues on the molecular surface of nsLTP2 are structurally similar to other plant defense proteins.

Selected figure(s)

Figure 3.
Fig. 3. A, stereo representation of the 15 best superimposed NMR structures of rice nsLTP2 (only the backbone atoms are shown for clarity). B, solution structure of rice nsLTP2. Disulfide bonds involved in the three-dimensional structure are shown in ball-and-stick representation. Helix I (green) and helix II (red) are connected through a loop (Gly17-Pro21). Helix II and helix III (purple) are joined by a sharp 90° turn. The region containing two single turn helices and the C terminus are shown in orange and brown, respectively.

Figure 5.
Fig. 5. A, schematic representations of the cysteine pairing patterns of nsLTP1 and nsLTP2 show high similarity except for the -CXC-motif. B, the side-chain orientations of nsLTP1 and nsLTP2 at the -CXC- motifs are shown with the ball-and-stick model. The hydrophilic Asn49 present in nsLTP1 is projected to the periphery of the protein, whereas the hydrophobic Phe^36 of nsLTP2 is buried inside the molecule.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 35267-35273) copyright 2002.

Figures were selected by an automated process.