High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings

Dong Hae Shin, Jae Young Lee, Kwang Yeon Hwang, Kyeong Kyu Kim, Se Won Suh

Research output: Contribution to journalArticle

195 Citations (Scopus)

Abstract

Background: The movement of lipids between membranes is aided by lipid-transfer proteins (LTPs). Some LTPs exhibit broad specificity, transferring many classes of lipids, and are termed non-specific LTPs (ns-LTPs). Despite their apparently similar mode of action, no sequence homology exists between mammalian and plant ns-LTPs and no three-dimensional structure has been reported for any plant ns-LTP. Results: We have determined the crystal structure of ns-LTP from maize seedlings by multiple isomorphous replacement and refined the structure to 1.9 Å resolution. The protein comprises a single compact domain with four α-helices and a long C-terminal region. The eight conserved cysteines form four disulfide bridges (assigned as Cys4-Cys52, Cys14-Cys29, Cys30-Cys75, and Cys50-Cys89) resolving the ambiguity that remained from the chemical determination of pairings in the homologous protein from castor bean. Two of the bonds, Cys4-Cys52 and Cys50-Cys89, differ from what would have been predicted from sequence alignment with soybean hydrophobic protein. The complex between maize ns-LTP and hexadecanoate (palmitate) has also been crystallized and its structure refined to 1.8 Å resolution. Conclusions: The fold of maize ns-LTP places it in a new category of all-α-type structure, first described for soybean hydrophobic protein. In the absence of a bound ligand, the protein has a tunnel-like hydrophobic cavity, which is large enough to accommodate a long fatty acyl chain. In the structure of the complex with palmitate, most of the acyl chain is buried inside this hydrophobic cavity.

Original languageEnglish
Pages (from-to)189-199
Number of pages11
JournalStructure
Volume3
Issue number2
Publication statusPublished - 1995 Dec 1
Externally publishedYes

Fingerprint

Palmitates
Seedlings
Zea mays
Castor Bean
Proteins
Sequence Alignment
Membrane Lipids
Sequence Homology
Disulfides
Cysteine
Ligands
Lipids
sterol carrier proteins
Glycine max HPS protein
lipid transfer protein

Keywords

  • Lipid-transfer protein
  • Maize protein
  • X-ray structure

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings. / Shin, Dong Hae; Lee, Jae Young; Hwang, Kwang Yeon; Kim, Kyeong Kyu; Suh, Se Won.

In: Structure, Vol. 3, No. 2, 01.12.1995, p. 189-199.

Research output: Contribution to journalArticle

Shin, Dong Hae ; Lee, Jae Young ; Hwang, Kwang Yeon ; Kim, Kyeong Kyu ; Suh, Se Won. / High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings. In: Structure. 1995 ; Vol. 3, No. 2. pp. 189-199.
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