› 1tuk

X-ray diffraction
1.12Å resolution

Crystal structure of liganded type 2 non specific lipid transfer protein from wheat

Released:
DOI: 10.2210/pdb1tuk/pdb
PDB entry 1tuk coloured by chain, front view.
PDB entry 1tuk coloured by chain, side view.
PDB entry 1tuk coloured by chain, top view.
Source organism: Triticum aestivum
Primary publication:
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 61 397-406 (2005)
PMID: 15805594

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160651 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Non-specific lipid-transfer protein 2G Chain: A
Molecule details ›
Chain: A
Length: 67 amino acids
Theoretical weight: 6.99 KDa
Source organism: Triticum aestivum
UniProt:
  • Canonical: P82900 (Residues: 30-96; Coverage: 100%)
Sequence domains: Protease inhibitor/seed storage/LTP family
Structure domains: Plant lipid-transfer and hydrophobic proteins

Ligands and Environments

2 bound ligands:
Ligand IOD 2 x IOD
Ligand PGM 2 x PGM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2
Unit cell:
a: 61.465Å b: 29.32Å c: 41.55Å
α: 90° β: 127.65° γ: 90°
R-values:
R R work R free
0.138 0.137 0.162

Quick links

Citations

4 review citations

The biochemistry and biology of extracellular plant lipid-transfer proteins (LTPs).
Yeats et al. (2008)
3 more

12 mentions without citation

Lipid transfer proteins: classification, nomenclature, structure, and function.
Salminen et al. (2016)
11 more